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Conserved domains on  [gi|188497750|ref|NP_277035|]
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hexokinase-1 isoform HKI-td [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 10-462 0e+00

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24124:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 473  Bit Score: 982.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  10 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 89
Cdd:cd24124   21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  90 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 169
Cdd:cd24124  101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 170 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 249
Cdd:cd24124  181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 250 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 329
Cdd:cd24124  261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 330 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 409
Cdd:cd24124  341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188497750 410 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 462
Cdd:cd24124  421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 466-899 0e+00

nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type I hexokinase.


:

Pssm-ID: 466977 [Multi-domain]  Cd Length: 434  Bit Score: 915.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 466 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 545
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24127   81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 705
Cdd:cd24127  161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 706 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 785
Cdd:cd24127  241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 786 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 865
Cdd:cd24127  321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 188497750 866 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 899
Cdd:cd24127  401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
 
Name Accession Description Interval E-value
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 10-462 0e+00

nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.


Pssm-ID: 466974 [Multi-domain]  Cd Length: 473  Bit Score: 982.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  10 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 89
Cdd:cd24124   21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  90 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 169
Cdd:cd24124  101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 170 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 249
Cdd:cd24124  181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 250 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 329
Cdd:cd24124  261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 330 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 409
Cdd:cd24124  341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188497750 410 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 462
Cdd:cd24124  421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 466-899 0e+00

nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type I hexokinase.


Pssm-ID: 466977 [Multi-domain]  Cd Length: 434  Bit Score: 915.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 466 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 545
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24127   81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 705
Cdd:cd24127  161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 706 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 785
Cdd:cd24127  241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 786 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 865
Cdd:cd24127  321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 188497750 866 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 899
Cdd:cd24127  401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
PTZ00107 PTZ00107
hexokinase; Provisional
 10-448 2.08e-108

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 342.43  E-value: 2.08e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  10 IDKYLYAMRLSDETLIDIMTRFRKEMKNGL-SRDFNPTA------TVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILR 82
Cdd:PTZ00107  11 LASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  83 VQVNH----EKNQN--VHMESEVYdTPENIV--HGSGSQLFDHVAECLGDFMEKRKIKD---KKLPVGFTFSFPCQQSKI 151
Cdd:PTZ00107  91 VSLRGggkmERTQSkfSLPKSALL-GEKGLLdkKATATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGFTFSFPCTQLSV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 152 DEAILITWTKRFKAS-----GVEGADVVKLLNKAIKkRGDYDANIVAVVNDTVGTMMTCGYDDQH----CEVGLIIGTGT 222
Cdd:PTZ00107 170 NNAILIDWTKGFETGratndPVEGKDVGELLNDAFK-RNNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVIIGTGS 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 223 NACYMEelrHIDLVEGDEGRMcINTEWGAFgdDGSLEdiRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMA 302
Cdd:PTZ00107 249 NACYFE---PEVSAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 303 KEGLLfegritPELLTRGKFNTSDVSAIEKNK-EGLHNAKEILTRL-GVEPSDDDCVSVQHVCTIVSFRSANLVAATLGA 380
Cdd:PTZ00107 321 QLKAP------PKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAA 394

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 381 ILNRLRdnkgTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPD--SDVRFLLSESGSGKGAAMVTAVA 448
Cdd:PTZ00107 395 PAKKTR----TVQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIAAMV 460
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 661-895 1.73e-106

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.


Pssm-ID: 461028  Cd Length: 236  Bit Score: 328.68  E-value: 1.73e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  661 EVGLIVGTGSNACYMEEMKNVEMVEGDQ---GQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMY 737
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  738 LGEIVRNILIDFTKKGFLFRGQiSETLKTRGIFETKFLSQIESDR-LALLQVRAILQQ-LGLNS-TCDDSILVKTVCGVV 814
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIETvTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  815 SRRAAQLCGAGMAAVVDKIRENRGldrlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPKCNVSFLLSEDGSGKGAALIT 893
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 188497750  894 AV 895
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 450-895 1.86e-102

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 326.63  E-value: 1.86e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 450 RLAEQHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLR-KQTHNNAV------VKMLPSFVRRTPDGTENGDFLALDLG 522
Cdd:PTZ00107   3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEaHRRHRNLWipnecsFKMLDSCVYNLPTGKEKGVYYAIDFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 523 GTNFRVLLVKIRSGKKrtVEMHNKIYAIPIEIMQG---------TGEELFDHIVSCISDFLDYMGIK---GPRMPLGFTF 590
Cdd:PTZ00107  83 GTNFRAVRVSLRGGGK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 591 SFPCQQTSLDAGILITWTKGFK----ATDCV-GHDVVTLLRDAIKRrEEFDLDVVAVVNDTVGTMMTCAYEE----PTCE 661
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFEtgraTNDPVeGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 662 VGLIVGTGSNACYMEEM----KNVEMVegdqgqmcINMEWGAFgdngCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMY 737
Cdd:PTZ00107 240 VGVIIGTGSNACYFEPEvsayGYAGTP--------INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAY 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 738 LGEIVRNILIDftkkgfLFRGQISETLKTRGIFETKFLSQIESDRLALLQ-VRAILQQL-GLNSTCDDSILVKTVCGVVS 815
Cdd:PTZ00107 308 LGEISRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSPDLQfSRQVIKEAwDVDLTDEDLYTIRKICELVR 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 816 RRAAQLCGAGMAAVVDKIRENRGLdrlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPK-CNVSFLLSEDGSGKGAALIT 893
Cdd:PTZ00107 382 GRAAQLAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIA 457


                 ..
gi 188497750 894 AV 895
Cdd:PTZ00107 458 AM 459
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 213-447 1.93e-100

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.


Pssm-ID: 461028  Cd Length: 236  Bit Score: 312.89  E-value: 1.93e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  213 EVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMY 289
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  290 LGELVRLILVKMAKEGLLFEGRiTPELLTRGKFNTSDVSAIEK-NKEGLHNAKEILTR-LGVE-PSDDDCVSVQHVCTIV 366
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESdPSEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  367 SFRSANLVAATLGAILNRLRDNKgtprlRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSD-VRFLLSESGSGKGAAMVT 445
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLGPGDkVVLVLAEDGSGVGAALIA 234


                  ..
gi 188497750  446 AV 447
Cdd:pfam03727 235 AV 236
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 1-448 3.67e-100

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 319.60  E-value: 3.67e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750   1 MAKRALHDFIDKYlyAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVrSIPDGS-EKGDFIALDLGGSSFR 79
Cdd:COG5026    1 MKKLLVDAFLKRH--GFDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  80 ILRVQVNheKNQNVHMESEVY----DTPENIvhgSGSQLFDHVAECLGDFmekrkiKDKKLPVGFTFSFPCQQSKIDEAI 155
Cdd:COG5026   75 VALVRFD--GEGTFEIENFKSfplpGTSSEI---TAEEFFDFIADYIEPL------LDESYKLGFCFSFPAEQLPDKDGR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 156 LITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQ----HCEVGLIIGTGTNACYMEELR 231
Cdd:COG5026  144 LIQWTKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNA 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 232 HIDLVEGDEGRMCINTEWGAFgdDGSLediRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGlLFEGR 311
Cdd:COG5026  224 PIGKLPAYEGPMIINMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 312 ITPELLTRGKFNTSDVSAIEKNKEGlhnAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLrDNKGT 391
Cdd:COG5026  298 FSEVFETPYSLTTVDMSRFLADPSD---EKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHL-GPGKT 373

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 392 PRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSD---VRFLLSESGSGKGAAMVTAVA 448
Cdd:COG5026  374 PLKPHCIAIDGSTYEKMPGLAEKIEYALQEYLLGEKgryVEFVLVENASLLGAAIAAALN 433
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 464-891 4.13e-92

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 298.02  E-value: 4.13e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 464 HFHLTKDMLLEVKKRMRAEMELGLRkqtHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsGKKRTVEM 543
Cdd:COG5026   14 GFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLGLPTGVKETGPVIALDAGGTNFRVALVRF--DGEGTFEI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 544 HNKIyAIPieiMQGTG-----EELFDHIVSCISDFLDYmgikgpRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVG 618
Cdd:COG5026   89 ENFK-SFP---LPGTSseitaEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 619 HDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTC----EVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCIN 694
Cdd:COG5026  159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIIN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 695 MEWGAFgdNGCLddiRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGfLFRGQISETLKTRGIFETKF 774
Cdd:COG5026  239 MESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 775 LSQI---ESDRLallqvrAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRlNVTVGVDGT 851
Cdd:COG5026  313 MSRFladPSDEK------EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-PHCIAIDGS 385

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 188497750 852 LYKLHPHF-SRIMHQTVKELSPKCN--VSFLLSEDGSGKGAAL 891
Cdd:COG5026  386 TYEKMPGLaEKIEYALQEYLLGEKGryVEFVLVENASLLGAAI 428
 
Name Accession Description Interval E-value
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 10-462 0e+00

nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.


Pssm-ID: 466974 [Multi-domain]  Cd Length: 473  Bit Score: 982.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  10 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 89
Cdd:cd24124   21 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  90 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 169
Cdd:cd24124  101 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVE 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 170 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 249
Cdd:cd24124  181 GADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEW 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 250 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 329
Cdd:cd24124  261 GAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 330 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 409
Cdd:cd24124  341 IEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHP 420

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188497750 410 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 462
Cdd:cd24124  421 QYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETL 473
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 466-899 0e+00

nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type I hexokinase.


Pssm-ID: 466977 [Multi-domain]  Cd Length: 434  Bit Score: 915.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 466 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 545
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24127   81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 705
Cdd:cd24127  161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 706 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 785
Cdd:cd24127  241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 786 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 865
Cdd:cd24127  321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 188497750 866 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 899
Cdd:cd24127  401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 466-898 0e+00

nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of types I to III hexokinases. Type I enzyme may have a catabolic function, producing H6P for energy production in glycolysis; it is bound to the mitochondrial membrane, which enables the coordination of glycolysis with the TCA cycle. Types II and III enzyme may have anabolic functions, providing H6P for glycogen or lipid synthesis.


Pssm-ID: 466941 [Multi-domain]  Cd Length: 433  Bit Score: 904.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 466 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 545
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24091   81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 705
Cdd:cd24091  161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 706 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 785
Cdd:cd24091  241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 786 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 865
Cdd:cd24091  321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                        410       420       430
                 ....*....|....*....|....*....|...
gi 188497750 866 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVR 898
Cdd:cd24091  401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 18-446 0e+00

nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of types I and II hexokinases.


Pssm-ID: 466939 [Multi-domain]  Cd Length: 429  Bit Score: 854.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 97
Cdd:cd24089    1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24089   81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24089  161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24089  241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24089  321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 446
Cdd:cd24089  401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 467-900 0e+00

nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type II hexokinase.


Pssm-ID: 466978 [Multi-domain]  Cd Length: 435  Bit Score: 808.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 467 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 546
Cdd:cd24128    2 LSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHNK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 547 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 626
Cdd:cd24128   82 IYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 627 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 706
Cdd:cd24128  162 EAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 707 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 786
Cdd:cd24128  242 DDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLALL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 787 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 866
Cdd:cd24128  322 QVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHET 401

                        410       420       430
                 ....*....|....*....|....*....|....
gi 188497750 867 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRLR 900
Cdd:cd24128  402 VKDLAPKCDVSFLQSEDGSGKGAALITAVACRIR 435
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 18-446 0e+00

nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the first two domains of HKDC1.


Pssm-ID: 466976 [Multi-domain]  Cd Length: 429  Bit Score: 797.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 97
Cdd:cd24126    1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24126   81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24126  161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24126  241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24126  321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 446
Cdd:cd24126  401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 467-899 0e+00

nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the second two domains of HKDC1.


Pssm-ID: 466980 [Multi-domain]  Cd Length: 433  Bit Score: 789.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 467 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKkRTVEMHNK 546
Cdd:cd24130    2 LTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGR-RSVRMYNK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 547 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 626
Cdd:cd24130   81 IFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDMLR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 627 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 706
Cdd:cd24130  161 EAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGCI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 707 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 786
Cdd:cd24130  241 DDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLALL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 787 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 866
Cdd:cd24130  321 QVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQET 400

                        410       420       430
                 ....*....|....*....|....*....|...
gi 188497750 867 VKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 899
Cdd:cd24130  401 VKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 466-894 0e+00

nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition.


Pssm-ID: 466869 [Multi-domain]  Cd Length: 427  Bit Score: 743.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 466 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGkkRTVEMHN 545
Cdd:cd24019    1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNGG--SQVKMES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24019   79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVE---MVEGDQGQMCINMEWGAFGD 702
Cdd:cd24019  159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEkwdGDEGDPGQVIINTEWGAFGD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 703 NGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESD- 781
Cdd:cd24019  239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDn 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 782 RLALLQVRAILQQLGLNS-TCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRenrgldRLNVTVGVDGTLYKLHPHFS 860
Cdd:cd24019  319 EGDFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 188497750 861 RIMHQTVKELSPK-CNVSFLLSEDGSGKGAALITA 894
Cdd:cd24019  393 KRMHETLKELVPPgCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 18-446 0e+00

nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type II hexokinase.


Pssm-ID: 466975 [Multi-domain]  Cd Length: 429  Bit Score: 733.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 97
Cdd:cd24125    1 RLSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24125   81 QIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24125  161 RKAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24125  241 LDDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24125  321 RKAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTA 446
Cdd:cd24125  401 TVRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK_meta cd24019
nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7. ...
 18-446 0e+00

nucleotide-binding domain (NBD) of metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition.


Pssm-ID: 466869 [Multi-domain]  Cd Length: 427  Bit Score: 713.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHekNQNVHMES 97
Cdd:cd24019    1 RLSDEQLEEIMDRLLKEMEKGLSKDTHPTASVKMLPTYVRSLPDGTENGDFLALDLGGTNFRVLLVTLNG--GSQVKMES 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24019   79 EIYAIPEEIMTGTGEQLFDYIAECLAEFLEKNGLKDKKLPLGFTFSFPCKQTGLDSATLVRWTKGFKCSGVEGEDVVRLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDL---VEGDEGRMCINTEWGAFGD 254
Cdd:cd24019  159 QEAIKRRGDIKVDVVAVVNDTVGTLMSCAYEDPNCEIGLIVGTGTNACYMEKLSNVEKwdgDEGDPGQVIINTEWGAFGD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 255 DGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNK 334
Cdd:cd24019  239 NGVLDFIRTEFDREVDEESLNPGKQLFEKMISGMYLGELVRLVLLKLAKEGLLFRGQLSEELLTRGSFETKYVSEIESDN 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 335 EG-LHNAKEILTRLGVEP-SDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRdnkgtpRLRTTVGVDGSLYKTHPQYS 412
Cdd:cd24019  319 EGdFSNTREILKELGLEDaSDEDCEIVRYVCEAVSTRAAQLVAAGIAALLNRMN------RKEVTVGVDGSLYKYHPKFH 392

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 188497750 413 RRFHKTLRRLVP-DSDVRFLLSESGSGKGAAMVTA 446
Cdd:cd24019  393 KRMHETLKELVPpGCKFKLMLSEDGSGKGAALVAA 427
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 467-898 0e+00

nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type III hexokinase.


Pssm-ID: 466979 [Multi-domain]  Cd Length: 430  Bit Score: 693.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 467 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsgKKRTVEMHNK 546
Cdd:cd24129    2 LSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHV---GTAGVQITSE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 547 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 626
Cdd:cd24129   79 IYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLLR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 627 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 706
Cdd:cd24129  159 EAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGCL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 707 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 786
Cdd:cd24129  239 AMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLALR 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 787 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 866
Cdd:cd24129  319 QVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQAT 398

                        410       420       430
                 ....*....|....*....|....*....|..
gi 188497750 867 VKELSPKCNVSFLLSEDGSGKGAALITAVGVR 898
Cdd:cd24129  399 VRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HK1-2_meta_rpt1 cd24089
nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from ...
 466-894 0e+00

nucleotide-binding domain (NBD) of the first repeat of types I and II hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of types I and II hexokinases.


Pssm-ID: 466939 [Multi-domain]  Cd Length: 429  Bit Score: 648.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 466 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 545
Cdd:cd24089    1 RLSDETLLDISRRFRKEMEKGLGKDTHPTATVKMLPTFVRSTPDGTEKGDFLALDLGGSNFRVLWVQVNDEKNQKVEMES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24089   81 QVYAIPEEIMHGSGTQLFDHVAECLADFMDKQKIKDKKLPLGFTFSFPCRQTKIDESILISWTKGFKASGVEGKDVVKLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 705
Cdd:cd24089  161 RKAIRRRGDYDIDIVAVVNDTVGTMMTCGYDDQNCEVGLIIGTGTNACYMEEMRNIDLVEGDEGRMCINTEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 706 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 785
Cdd:cd24089  241 LEDIRTEFDREIDRGSLNPGKQLFEKMISGMYLGELVRLILVKMAKEGLLFGGKISPELLTRGKFETKDVSAIEKEKEGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 786 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 865
Cdd:cd24089  321 ANAKEILTRLGLDPSEDDCVNVQHVCTIVSFRSANLCAATLAAILTRLRENKGLERLRTTVGVDGSVYKKHPQFSKRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 188497750 866 TVKELSPKCNVSFLLSEDGSGKGAALITA 894
Cdd:cd24089  401 AVRRLVPDCDVRFLLSEDGSGKGAAMVTA 429
ASKHA_NBD_HKDC1_meta_rpt1 cd24126
nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 ...
 466-894 0e+00

nucleotide-binding domain (NBD) of the first repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the first two domains of HKDC1.


Pssm-ID: 466976 [Multi-domain]  Cd Length: 429  Bit Score: 602.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 466 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 545
Cdd:cd24126    1 RLSDDTLLDIMTRFRAEMEKGLAKDTNPTAAVKMLPTFVRSIPDGSEKGDFLALDLGGSKFRVLRVKVSEDGKQKVQMES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24126   81 QFYPTPEEIIHGTGTELFDYVAECLADFMKKKGIKHKKLPLGFTFSFPCRQTKLDEGVLISWTKNFKARGVQGTDVVSSL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 705
Cdd:cd24126  161 RKAIRKHKDVDVDVLALVNDTVGTMMTCGYDDQYCEVGVIIGTGTNACYMEEMSHIDLVEGDEGRMCINTEWGAFGDDGS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 706 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 785
Cdd:cd24126  241 LEDIRTEFDREIDLGSLNPGKQLFEKMISGLYMGELVRLILLKMAKKGLLFKGQISPALRTKGKIETKHVAAIEKYKEGL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 786 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQ 865
Cdd:cd24126  321 YNTREILSDLGLEPSEEDCIAVQHVCTIVSFRSANLCAAALAAILTRLRENKKLERLRTTVGMDGTVYKTHPQYAKRLHK 400

                        410       420
                 ....*....|....*....|....*....
gi 188497750 866 TVKELSPKCNVSFLLSEDGSGKGAALITA 894
Cdd:cd24126  401 VVRRLVPSCDVRFLLSESGSGKGAAMVTA 429
ASKHA_NBD_HK2_meta_rpt1 cd24125
nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan ...
 467-894 0e+00

nucleotide-binding domain (NBD) of the first repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type II hexokinase.


Pssm-ID: 466975 [Multi-domain]  Cd Length: 429  Bit Score: 599.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 467 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 546
Cdd:cd24125    2 LSDETLLEISKRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVSDNGLQKVEMENQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 547 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 626
Cdd:cd24125   82 IYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVALLR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 627 DAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCL 706
Cdd:cd24125  162 KAIQKRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGTNACYMEEMRHIDLVEGDEGRMCINMEWGAFGDDGSL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 707 DDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALL 786
Cdd:cd24125  242 DDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKEELLFGGKLSPELLNTGHFETKDVSDIEGEKDGIR 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 787 QVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQT 866
Cdd:cd24125  322 KAREVLMRLGLDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFARRLHKT 401

                        410       420
                 ....*....|....*....|....*...
gi 188497750 867 VKELSPKCNVSFLLSEDGSGKGAALITA 894
Cdd:cd24125  402 VRRLVPGCDVRFLRSEDGSGKGAAMVTA 429
ASKHA_NBD_HK1-3_meta_rpt2 cd24091
nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from ...
 18-450 0e+00

nucleotide-binding domain (NBD) of the second repeat of types I, II, and III hexokinases from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of types I to III hexokinases. Type I enzyme may have a catabolic function, producing H6P for energy production in glycolysis; it is bound to the mitochondrial membrane, which enables the coordination of glycolysis with the TCA cycle. Types II and III enzyme may have anabolic functions, providing H6P for glycogen or lipid synthesis.


Pssm-ID: 466941 [Multi-domain]  Cd Length: 433  Bit Score: 584.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 97
Cdd:cd24091    1 QLSHDQLLEVKARMRAEMERGLRKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVKVRSGKWRGVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24091   81 KIYAIPQEIMQGTGEELFDHIVQCIADFLEYMGLKGVSLPLGFTFSFPCQQTSLDEGILLKWTKGFKATDCEGEDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24091  161 REAIKRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEIGLIVGTGSNACYMEEMRNVEMVEGEEGRMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24091  241 LDDIRTRYDVEVDELSLNPGKQRFEKMISGMYLGEIVRNILIDLTKRGLLFRGQISERLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24091  321 LQVRAILQQLGLDSTCDDSIIVKEVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRVMHE 400

                        410       420       430
                 ....*....|....*....|....*....|...
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 450
Cdd:cd24091  401 TVKELAPKCDVTFLQSEDGSGKGAALITAVACR 433
ASKHA_NBD_HK1_meta_rpt1 cd24124
nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan ...
 447-899 0e+00

nucleotide-binding domain (NBD) of the first repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type I hexokinase.


Pssm-ID: 466974 [Multi-domain]  Cd Length: 473  Bit Score: 580.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 447 VAYRLAE----QHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLG 522
Cdd:cd24124    6 LAYYFTElkddQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 523 GTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAG 602
Cdd:cd24124   86 GSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 603 ILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVE 682
Cdd:cd24124  166 ILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHID 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 683 MVEGDQGQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISE 762
Cdd:cd24124  246 LVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITP 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 763 TLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRL 842
Cdd:cd24124  326 ELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRL 405

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 188497750 843 NVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 899
Cdd:cd24124  406 RTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 462
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 457-898 0e+00

nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to type IV hexokinase. It is found in the liver and pancreatic beta-cells, where it is controlled by insulin (activation) and glucagon (inhibition). In pancreatic beta-cells, type IV enzyme acts as a glucose sensor to modify insulin secretion. Mutations in type IV hexokinase have been associated with diabetes mellitus.


Pssm-ID: 466942 [Multi-domain]  Cd Length: 444  Bit Score: 569.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 457 QIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSG 536
Cdd:cd24092    1 LVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 537 KKR--TVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKAT 614
Cdd:cd24092   81 EEGqwSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKAS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 615 DCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCIN 694
Cdd:cd24092  161 GAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 695 MEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKF 774
Cdd:cd24092  241 TEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRF 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 775 LSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYK 854
Cdd:cd24092  321 VSQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYK 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 188497750 855 LHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVR 898
Cdd:cd24092  401 LHPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK2_meta_rpt2 cd24128
nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan ...
 18-451 0e+00

nucleotide-binding domain (NBD) of the second repeat of type II hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type II hexokinase.


Pssm-ID: 466978 [Multi-domain]  Cd Length: 435  Bit Score: 564.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 97
Cdd:cd24128    1 QLSHDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVRSTPDGTEKGDFLALDLGGTNFRVLLVRVRNGKWRGVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24128   81 KIYAIPQEVMHGTGEELFDHIVHCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDEGILLKWTKGFKASGCEGEDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24128  161 KEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24128  241 LDDFRTEFDVAVDELSLNPGKQRYEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24128  321 LQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHE 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 451
Cdd:cd24128  401 TVKDLAPKCDVSFLQSEDGSGKGAALITAVACRI 434
ASKHA_NBD_HK1_meta_rpt2 cd24127
nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan ...
 18-451 0e+00

nucleotide-binding domain (NBD) of the second repeat of type I hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type I hexokinase.


Pssm-ID: 466977 [Multi-domain]  Cd Length: 434  Bit Score: 545.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMES 97
Cdd:cd24127    1 HLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRSTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24127   81 KIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCEGHDVVTLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24127  161 RDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24127  241 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLAL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24127  321 LQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDHLNVTVGVDGTLYKLHPHFSRIMHQ 400

                        410       420       430
                 ....*....|....*....|....*....|....
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 451
Cdd:cd24127  401 TVKELSPKCNVSFLLSEDGSGKGAALITAVGVRL 434
ASKHA_NBD_HK3_meta_rpt2 cd24129
nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan ...
 18-450 0e+00

nucleotide-binding domain (NBD) of the second repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the second two domains of type III hexokinase.


Pssm-ID: 466979 [Multi-domain]  Cd Length: 430  Bit Score: 541.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEknqNVHMES 97
Cdd:cd24129    1 QLSHDQLAAVQAQMRKEMAKGLRGETHAAASVRMLPTYVRATPDGSERGDFLALDLGGTNFRVLLVHVGTA---GVQITS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24129   78 EIYSIPETVAQGTGQQLFDHIVDCIVDFQQKQGLSGQSLPLGFTFSFPCRQLGLDQGILLNWTKGFKASGCVGQDVVSLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24129  158 REAATRKQAVELNVVAIVNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGDNGC 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24129  238 LAMISTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGKQIQRLQTRDIFKTKFLSEIESDSLAL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24129  318 RQVRAILEDLGLPLTSDDALLVLEVCQTVSQRAAQLCAAGVAAVVEKMRENRGLDELAVTVGVDGTLYKLHPRFSSLVQA 397

                        410       420       430
                 ....*....|....*....|....*....|...
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 450
Cdd:cd24129  398 TVRELAPRCVVTFLQSEDGSGKGAALVTAVACR 430
ASKHA_NBD_HKDC1_meta_rpt2 cd24130
nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 ...
 18-451 0e+00

nucleotide-binding domain (NBD) of the second repeat of hexokinase domain-containing protein 1 (HKDC1) from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. HKDC1 is a putative novel fifth hexokinase found in vertebrates. It may be involved in whole-body glucose use. The model corresponds to the second two domains of HKDC1.


Pssm-ID: 466980 [Multi-domain]  Cd Length: 433  Bit Score: 539.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  18 RLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNqNVHMES 97
Cdd:cd24130    1 QLTRDQLQEVKQKMRTELEYGLKKETHPTASVKMLPTYVYGTPDGTEKGKFLALDLGGTNFRVLLVKIRSGRR-SVRMYN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  98 EVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24130   80 KIFAIPLEIMQGTGEELFDHIVQCIADFLDYMGLKGARLPLGFTFSFPCRQTGIDKGTLVGWTKGFKATDCEGEDVVDML 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGS 257
Cdd:cd24130  160 REAIKRRNEFDLDIVAVVNDTVGTMMTCGYEDPKCEIGLIAGTGSNVCYMEEMRNIEIVEGDEGRMCINTEWGGFGDNGC 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 258 LEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGL 337
Cdd:cd24130  240 IDDIRTRYDREVDEGSLNPGKQRYEKMTSGMYLGEIVRQILIDLTKQGLLFRGQISERLRTRGIFETKFLSQIESDRLAL 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 338 HNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHK 417
Cdd:cd24130  320 LQVRRILQQLGLDSTCEDSIIVKEVCGAVSRRAAQLCGAGLAAIVEKIRENQGLDRLDITVGVDGTLYKLHPHFSRILQE 399

                        410       420       430
                 ....*....|....*....|....*....|....
gi 188497750 418 TLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRL 451
Cdd:cd24130  400 TVKELAPQCDVTFMLSEDGSGKGAALITAVAKRL 433
ASKHA_NBD_HK4_meta cd24092
nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain ...
 10-450 3.63e-179

nucleotide-binding domain (NBD) of type IV hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to type IV hexokinase. It is found in the liver and pancreatic beta-cells, where it is controlled by insulin (activation) and glucagon (inhibition). In pancreatic beta-cells, type IV enzyme acts as a glucose sensor to modify insulin secretion. Mutations in type IV hexokinase have been associated with diabetes mellitus.


Pssm-ID: 466942 [Multi-domain]  Cd Length: 444  Bit Score: 524.83  E-value: 3.63e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  10 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV--NH 87
Cdd:cd24092    2 VEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVgeGE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  88 EKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASG 167
Cdd:cd24092   82 EGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 168 VEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINT 247
Cdd:cd24092  162 AEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 248 EWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDV 327
Cdd:cd24092  242 EWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGELVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 328 SAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKT 407
Cdd:cd24092  322 SQVESDTGDRKQIYNILSTLGLRPSTTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKL 401

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 188497750 408 HPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYR 450
Cdd:cd24092  402 HPSFKERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACK 444
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 469-892 4.45e-165

nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.


Pssm-ID: 466868 [Multi-domain]  Cd Length: 431  Bit Score: 487.91  E-value: 4.45e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 469 KDMLLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKiY 548
Cdd:cd24018    1 VSKLEEIVKHFLSEMEKGLEGDGGS---LPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFIIVQRK-Y 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 549 AIPIEIMQGTGEELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLL 625
Cdd:cd24018   77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 626 RDAIKRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVE------GDQGQMCINMEWGA 699
Cdd:cd24018  157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIKKLTspsgsvTKSDEMIINTEWGA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 700 FGDNGCLDDiRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIE 779
Cdd:cd24018  236 FDNEREVLP-LTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRIE 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 780 SDRLALLQ-VRAILQQLG--LNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenRGLDRLN-VTVGVDGTLYKL 855
Cdd:cd24018  315 ADTSPDLDaVRDILKELLaiDNTTLEDRKLIKRICELVSTRAARLSAAAIAAILLK----RGSLLPEpVTVGIDGSVYEK 390

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 188497750 856 HPHFSRIMHQTVKELSP---KCNVSFLLSEDGSGKGAALI 892
Cdd:cd24018  391 YPGFKDRLSEALRELFGpevKANISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 467-894 3.99e-159

nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type III hexokinase.


Pssm-ID: 466940 [Multi-domain]  Cd Length: 431  Bit Score: 472.87  E-value: 3.99e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 467 LTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLG--GTNFRVLLVKIRSGKKRTVEMH 544
Cdd:cd24090    2 VTRAQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 545 NKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTL 624
Cdd:cd24090   82 SQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 625 LRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNG 704
Cdd:cd24090  162 LRDAIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 705 CLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLA 784
Cdd:cd24090  242 ALGPVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 785 LLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMH 864
Cdd:cd24090  322 AARVRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQ 401

                        410       420       430
                 ....*....|....*....|....*....|
gi 188497750 865 QTVKELSPKCNVSFLLSEDGSGKGAALITA 894
Cdd:cd24090  402 GTVMLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK3_meta_rpt1 cd24090
nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan ...
 22-446 2.58e-152

nucleotide-binding domain (NBD) of the first repeat of type III hexokinase from metazoan hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. For example, members from vertebrates contain four hexokinase isozymes, designated I to IV, where types I to III contain a duplication of the two-domain yeast-type hexokinases. Both the N- and C-terminal halves bind hexose and H6P. In types I and III only the C-terminal half supports catalysis. Their N-terminal half is the regulatory region. In type II, both halves support catalysis. Type IV hexokinase is similar to the yeast enzyme in containing only the two domains and is sometimes incorrectly referred to as glucokinase. Whereas types I to III can phosphorylate a variety of hexose sugars and are inhibited by glucose-6-phosphate (G6P), type IV is specific for glucose and shows no G6P inhibition. The model corresponds to the first two domains of type III hexokinase.


Pssm-ID: 466940 [Multi-domain]  Cd Length: 431  Bit Score: 455.15  E-value: 2.58e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  22 ETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLG--GSSFRILRVQVNHEKNQNVHMESEV 99
Cdd:cd24090    5 AQLQQIQASLLGSMEQALRGQASPAPAVRMLPTYVGSTPHGTEKGDFVVLELGatGASLRVLWVTLTGIEGHRVEPRSQE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 100 YDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNK 179
Cdd:cd24090   85 FVIPQEVMLGAGQQLFDFAAHCLSEFLDGQPVPKQGLQLGFSFSFPCHQTGLDRSTLISWTKGFRCSDVEGQDVVQLLRD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 180 AIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLE 259
Cdd:cd24090  165 AIQRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVGLVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSFSDDGALG 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 260 DIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHN 339
Cdd:cd24090  245 PVLTTFDHTLDHESLNPGAQRFEKMIGGLYLGELVRLVLVHLAQRGVLFGGSTSPALRSQGSILLEHVAEMEDPSAGAAR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 340 AKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTL 419
Cdd:cd24090  325 VRAILQDLGLSPSASDVELVQHVCRAVCTRAAQLCAAALAAVLSHLQHSREQQTLQVAVATGGRVCERHPRFCSILQGTV 404

                        410       420
                 ....*....|....*....|....*..
gi 188497750 420 RRLVPDSDVRFLLSESGSGKGAAMVTA 446
Cdd:cd24090  405 MLLAPECDVSFIPSVDGGGRGVAMVTA 431
ASKHA_NBD_HK_fungi cd24018
nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1. ...
 21-444 1.61e-148

nucleotide-binding domain (NBD) of fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar.


Pssm-ID: 466868 [Multi-domain]  Cd Length: 431  Bit Score: 445.54  E-value: 1.61e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  21 DETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVhMESEVY 100
Cdd:cd24018    1 VSKLEEIVKHFLSEMEKGLEGD---GGSLPMLPSFVTERPTGKETGTYLALDLGGTNLRVCLVTLDGNGGIFI-IVQRKY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 101 DTPENIVHGSGSQLFDHVAECLGDFMEKRKIK---DKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24018   77 KIPDEAKTGTGEELFDFIAECIAEFLEEHNLDlqsDKTIPLGFTFSFPVQQTSIDSGILISWTKGFNAPGVVGKDVVELL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHI---DLVEG---DEGRMCINTEWGA 251
Cdd:cd24018  157 QNALDRRG-VNVKVVALVNDTVGTLVASAYFDPSTVIGVIFGTGTNACYWEKVSNIkklTSPSGsvtKSDEMIINTEWGA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 252 FgdDGSLEDI-RTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAI 330
Cdd:cd24018  236 F--DNEREVLpLTKYDRELDDASPNPGQQRFEKMISGMYLGELVRLILLDLIDRGLLFSGKSSELLNEPYSLDTAFLSRI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 331 EKNKEG-LHNAKEILTRLGV--EPSDDDCVSVQHVCTIVSFRSANLVAATLGAILnrLRDNKGTPRlRTTVGVDGSLYKT 407
Cdd:cd24018  314 EADTSPdLDAVRDILKELLAidNTTLEDRKLIKRICELVSTRAARLSAAAIAAIL--LKRGSLLPE-PVTVGIDGSVYEK 390

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 188497750 408 HPQYSRRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMV 444
Cdd:cd24018  391 YPGFKDRLSEALRELFGPEvkaNISLVLAKDGSGLGAAII 430
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 469-893 3.39e-138

nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466850 [Multi-domain]  Cd Length: 357  Bit Score: 415.91  E-value: 3.39e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 469 KDMLLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSgkKRTVEMHNKIY 548
Cdd:cd24000    1 DEDLKEITDAFLEELEKGLAGEPSS---LKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLDG--KGIEVTISKKY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 549 AIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPrMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDA 628
Cdd:cd24000   76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLKKP-LPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 629 IKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNvemVEGDQGQMCINMEWGAFGDNgclDD 708
Cdd:cd24000  155 LKKR-GLPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSN---ILLGDGGMIINTEWGNFGKN---SL 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 709 IRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKgflfrgqisetlktrgifetkflsqiesdrlallqv 788
Cdd:cd24000  228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 789 railqqlglnstcddsiLVKTVCGVVSRRAAQLCGAGMAAVVDKIRENrglDRLNVTVGVDGTLYKLHPHFSRIMHQTVK 868
Cdd:cd24000  272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331

                        410       420
                 ....*....|....*....|....*.
gi 188497750 869 ELSPK-CNVSFLLSEDGSGKGAALIT 893
Cdd:cd24000  332 ELLGRgIRIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 21-445 5.91e-134

nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466850 [Multi-domain]  Cd Length: 357  Bit Score: 404.74  E-value: 5.91e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  21 DETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVHMESEVY 100
Cdd:cd24000    1 DEDLKEITDAFLEELEKGLAGE---PSSLKMLPSYVSPLPTGLESGEFLAIDLGGTNLRVALVSLD--GKGIEVTISKKY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 101 DTPENIVHGSGSQLFDHVAECLGDFMEKRKIKdKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKA 180
Cdd:cd24000   76 EIPDEIKTASAEEFFDFIADCIAEFLKENGLK-KPLPLGFTFSFPLEQTSLNDGKLLSWTKGFKIPGVEGKDVGELLNDA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 181 IKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDlveGDEGRMCINTEWGAFGDDgslED 260
Cdd:cd24000  155 LKKRG-LPVKVVAVLNDTVATLLAGAYKDPDCRIGLILGTGTNAAYLEPTSNIL---LGDGGMIINTEWGNFGKN---SL 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 261 IRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEgllfegritpelltrgkfntsdvsaieknkeglhna 340
Cdd:cd24000  228 PRTEYDREVDKASENPGFQPLEKMVSGKYLGELVRLILKDLADE------------------------------------ 271

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 341 keiltrlgvepsdddcvSVQHVCTIVSFRSANLVAATLGAILNRLRDNkgtPRLRTTVGVDGSLYKTHPQYSRRFHKTLR 420
Cdd:cd24000  272 -----------------ILRKICELVAERSARLAAAAIAALLRKTGDS---PEKKITIAVDGSLFEKYPGYRERLEEYLK 331

                        410       420
                 ....*....|....*....|....*.
gi 188497750 421 RLVP-DSDVRFLLSESGSGKGAAMVT 445
Cdd:cd24000  332 ELLGrGIRIELVLVEDGSLIGAALAA 357
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 22-448 6.81e-123

nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.


Pssm-ID: 466870 [Multi-domain]  Cd Length: 439  Bit Score: 379.31  E-value: 6.81e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  22 ETLIDIMTrfrKEMKNGLSRDfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYD 101
Cdd:cd24020    7 RQVADAMV---VEMEAGLASE--GGSKLKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYEEVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 102 TPENIVHGSGSQLFDHVAECLGDFMEK----RKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLL 177
Cdd:cd24020   82 IPPELMVGTSEELFDFIAGELAKFVATegegFHPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVVELL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 178 NKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFgD 254
Cdd:cd24020  162 EEALERQG-LDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGlprSGEMVINTEWGNF-R 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 255 DGSLEdiRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAI-EKN 333
Cdd:cd24020  240 SSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMhEDD 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 334 KEGLHNAKEILTR-LGVEPSD-DDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDNKG-TPRLRTTVGVDGSLYKTHP 409
Cdd:cd24020  318 SPDLETVARILKDaLGIDDTSlEARKVVVEVCDLVAERGARLAAAGIVGILKKLgRDGGGsSPAQRTVVAVDGGLYEHYP 397

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 188497750 410 QYSRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTAVA 448
Cdd:cd24020  398 KFREYMQQALVELLGDeaaDSVELELSNDGSGIGAALLAAAH 439
ASKHA_NBD_HK_plant cd24020
nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 467-894 1.05e-122

nucleotide-binding domain (NBD) of plant hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases act as sugar sensors in higher plants. They may regulate sugar-dependent gene repression or activation. They mediate the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. They may also regulate the execution of program cell death in plant cells, as well as promote roots and leaves growth.


Pssm-ID: 466870 [Multi-domain]  Cd Length: 439  Bit Score: 378.93  E-value: 1.05e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 467 LTKDMLLEVKKRMRAEMELGLRKQTHNNavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNK 546
Cdd:cd24020    1 TPVSRLRQVADAMVVEMEAGLASEGGSK--LKMLPSYVDNLPSGDEKGLFYALDLGGTNFRVLRVQLGGKEGRVDKQEYE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 547 IYAIPIEIMQGTGEELFDHIVSCISDFLDYMG----IKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVV 622
Cdd:cd24020   79 EVPIPPELMVGTSEELFDFIAGELAKFVATEGegfhPEGEKRELGFTFSFPVKQTSIDSGTLIKWTKGFTISDTVGKDVV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 623 TLLRDAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQ---GQMCINMEWGA 699
Cdd:cd24020  159 ELLEEALERQ-GLDMRVAALVNDTVGTLAGGRYVDQDTMAAVILGTGTNAAYVERADAIPKWSGGLprsGEMVINTEWGN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 700 FgDNGCLDdiRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIE 779
Cdd:cd24020  238 F-RSSHLP--RTEEDRELDAESLNPGEQIFEKMISGMYLGEIVRRVLLRMAEEAALFGDTVPSKLEIPFILRTPDMSAMH 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 780 SDRLA-LLQVRAILQQ-LGL-NSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLN--VTVGVDGTLYK 854
Cdd:cd24020  315 EDDSPdLETVARILKDaLGIdDTSLEARKVVVEVCDLVAERGARLAAAGIVGILKKLGRDGGGSSPAqrTVVAVDGGLYE 394

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 188497750 855 LHPHFSRIMHQTVKELSPKC---NVSFLLSEDGSGKGAALITA 894
Cdd:cd24020  395 HYPKFREYMQQALVELLGDEaadSVELELSNDGSGIGAALLAA 437
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 472-894 1.16e-116

nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.


Pssm-ID: 466937 [Multi-domain]  Cd Length: 428  Bit Score: 362.46  E-value: 1.16e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 472 LLEVKKRMRAEMELGLRKQTHNnavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsGKKRTVEMHNKIYAIP 551
Cdd:cd24087    4 LRKITDHFISELEKGLSKKGGN---IPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKL--GGNGKFDITQSKYRLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 552 IEIMQGTGEELFDHIVSCISDFLD--YMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAI 629
Cdd:cd24087   79 EELKTGTGEELWDFIADCLKKFVEehFPGGKSEPLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQKAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 630 KRREeFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVE----GDQGQMCINMEWGAFgDNGC 705
Cdd:cd24087  159 KKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEVVSNIPKLEhddiPPDSPMAINCEYGAF-DNEH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 706 LDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLA- 784
Cdd:cd24087  237 LVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEEDPFEn 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 785 LLQVRAILQQ-LGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKirenRGLDRLNvtVGVDGTLYKLHPHFSRIM 863
Cdd:cd24087  317 LEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK----RGYKTCH--VAADGSVYNKYPGFKERA 390

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 188497750 864 HQTVKEL----SPKCNVSFLLSEDGSGKGAALITA 894
Cdd:cd24087  391 AQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAA 425
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 472-892 1.29e-111

nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 (GLK-2) from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (also known as glucokinase-1, EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to glucokinase-1 and glucokinase-2.


Pssm-ID: 466938 [Multi-domain]  Cd Length: 445  Bit Score: 350.16  E-value: 1.29e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 472 LLEVKKRMRAEMELGLrkqTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrSGKkRTVEMHNKIYAIP 551
Cdd:cd24088    4 LDKLTAEFQRQMEKGL---AKHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVEL-HGD-GTFSLRQEKSKIP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 552 IEIMQG-TGEELFDHIVSCISDFL-DY------MGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVT 623
Cdd:cd24088   79 DELKTGvTAKDLFDYLAKSVEAFLtKHhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKDVVK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 624 LLRDAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCE---VGLIVGTGSNACYMEEMKNV------EMVEGDQGQMCIN 694
Cdd:cd24088  159 LLQDELDRQ-GIPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklddsSRVGKGKTHMVIN 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 695 MEWGAFgdngclDDIRTH-----YDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFL---FRGQISETLKT 766
Cdd:cd24088  238 TEWGSF------DNELKVlpttpYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNT 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 767 RGIFETKFLSQIESDRLALLQV--RAILQQLGLNS-TCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLN 843
Cdd:cd24088  312 PYGLDTAVLSAIEIDSEAELRAtrKVLLDDLGLPApSLEDAEAVRKISRAIGRRAARLSAVAIAAILIKTGALNKSYDGE 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 188497750 844 VTVGVDGTLYKLHPHFSRIMHQTVKELSP----KCNVSFLLSEDGSGKGAALI 892
Cdd:cd24088  392 INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
PTZ00107 PTZ00107
hexokinase; Provisional
 10-448 2.08e-108

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 342.43  E-value: 2.08e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  10 IDKYLYAMRLSDETLIDIMTRFRKEMKNGL-SRDFNPTA------TVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILR 82
Cdd:PTZ00107  11 LASLVNQFTMSKEKLKELVDYFLYELVEGLeAHRRHRNLwipnecSFKMLDSCVYNLPTGKEKGVYYAIDFGGTNFRAVR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  83 VQVNH----EKNQN--VHMESEVYdTPENIV--HGSGSQLFDHVAECLGDFMEKRKIKD---KKLPVGFTFSFPCQQSKI 151
Cdd:PTZ00107  91 VSLRGggkmERTQSkfSLPKSALL-GEKGLLdkKATATDLFDHIAKSIKKMMEENGDPEdlnKPVPVGFTFSFPCTQLSV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 152 DEAILITWTKRFKAS-----GVEGADVVKLLNKAIKkRGDYDANIVAVVNDTVGTMMTCGYDDQH----CEVGLIIGTGT 222
Cdd:PTZ00107 170 NNAILIDWTKGFETGratndPVEGKDVGELLNDAFK-RNNVPANVVAVLNDTVGTLISCAYQKPKntppCQVGVIIGTGS 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 223 NACYMEelrHIDLVEGDEGRMcINTEWGAFgdDGSLEdiRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMA 302
Cdd:PTZ00107 249 NACYFE---PEVSAYGYAGTP-INMECGNF--DSKLP--ITPYDLEMDWYTPNRGRQQFEKMISGAYLGEISRRLIVHLL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 303 KEGLLfegritPELLTRGKFNTSDVSAIEKNK-EGLHNAKEILTRL-GVEPSDDDCVSVQHVCTIVSFRSANLVAATLGA 380
Cdd:PTZ00107 321 QLKAP------PKMWQSGSFESEDASMILNDQsPDLQFSRQVIKEAwDVDLTDEDLYTIRKICELVRGRAAQLAAAFIAA 394

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 381 ILNRLRdnkgTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPD--SDVRFLLSESGSGKGAAMVTAVA 448
Cdd:PTZ00107 395 PAKKTR----TVQGKATVAIDGSVYVKNPWFRRLLQEYINSILGPdaGNVVFYLADDGSGKGAAIIAAMV 460
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 661-895 1.73e-106

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.


Pssm-ID: 461028  Cd Length: 236  Bit Score: 328.68  E-value: 1.73e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  661 EVGLIVGTGSNACYMEEMKNVEMVEGDQ---GQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMY 737
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKLpksGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  738 LGEIVRNILIDFTKKGFLFRGQiSETLKTRGIFETKFLSQIESDR-LALLQVRAILQQ-LGLNS-TCDDSILVKTVCGVV 814
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESDPsEDLETTREILEElLGIETvTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  815 SRRAAQLCGAGMAAVVDKIRENRGldrlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPKCNVSFLLSEDGSGKGAALIT 893
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDKK-----VTVGVDGSVYEKYPGFRERLQEALRElLGPGDKVVLVLAEDGSGVGAALIA 234


                  ..
gi 188497750  894 AV 895
Cdd:pfam03727 235 AV 236
PTZ00107 PTZ00107
hexokinase; Provisional
 450-895 1.86e-102

hexokinase; Provisional


Pssm-ID: 240270 [Multi-domain]  Cd Length: 464  Bit Score: 326.63  E-value: 1.86e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 450 RLAEQHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLR-KQTHNNAV------VKMLPSFVRRTPDGTENGDFLALDLG 522
Cdd:PTZ00107   3 RYIKQRVRLASLVNQFTMSKEKLKELVDYFLYELVEGLEaHRRHRNLWipnecsFKMLDSCVYNLPTGKEKGVYYAIDFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 523 GTNFRVLLVKIRSGKKrtVEMHNKIYAIPIEIMQG---------TGEELFDHIVSCISDFLDYMGIK---GPRMPLGFTF 590
Cdd:PTZ00107  83 GTNFRAVRVSLRGGGK--MERTQSKFSLPKSALLGekglldkkaTATDLFDHIAKSIKKMMEENGDPedlNKPVPVGFTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 591 SFPCQQTSLDAGILITWTKGFK----ATDCV-GHDVVTLLRDAIKRrEEFDLDVVAVVNDTVGTMMTCAYEE----PTCE 661
Cdd:PTZ00107 161 SFPCTQLSVNNAILIDWTKGFEtgraTNDPVeGKDVGELLNDAFKR-NNVPANVVAVLNDTVGTLISCAYQKpkntPPCQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 662 VGLIVGTGSNACYMEEM----KNVEMVegdqgqmcINMEWGAFgdngCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMY 737
Cdd:PTZ00107 240 VGVIIGTGSNACYFEPEvsayGYAGTP--------INMECGNF----DSKLPITPYDLEMDWYTPNRGRQQFEKMISGAY 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 738 LGEIVRNILIDftkkgfLFRGQISETLKTRGIFETKFLSQIESDRLALLQ-VRAILQQL-GLNSTCDDSILVKTVCGVVS 815
Cdd:PTZ00107 308 LGEISRRLIVH------LLQLKAPPKMWQSGSFESEDASMILNDQSPDLQfSRQVIKEAwDVDLTDEDLYTIRKICELVR 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 816 RRAAQLCGAGMAAVVDKIRENRGLdrlnVTVGVDGTLYKLHPHFSRIMHQTVKE-LSPK-CNVSFLLSEDGSGKGAALIT 893
Cdd:PTZ00107 382 GRAAQLAAAFIAAPAKKTRTVQGK----ATVAIDGSVYVKNPWFRRLLQEYINSiLGPDaGNVVFYLADDGSGKGAAIIA 457


                 ..
gi 188497750 894 AV 895
Cdd:PTZ00107 458 AM 459
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 22-448 1.38e-100

nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.


Pssm-ID: 466937 [Multi-domain]  Cd Length: 428  Bit Score: 320.48  E-value: 1.38e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  22 ETLIDIMTRFRKEMKNGLSRdfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVhMESEvYD 101
Cdd:cd24087    2 ERLRKITDHFISELEKGLSK---KGGNIPMIPTWVMGFPTGKETGDYLALDLGGTNLRVCLVKLGGNGKFDI-TQSK-YR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 102 TPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKK--LPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNK 179
Cdd:cd24087   77 LPEELKTGTGEELWDFIADCLKKFVEEHFPGGKSepLPLGFTFSYPASQDKINHGILQRWTKGFDIPNVEGHDVVPMLQK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 180 AIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYME------ELRHIDLVEGDEgrMCINTEWGAFg 253
Cdd:cd24087  157 ALKKRN-VPIELVALINDTTGTLIASNYTDPETKIGVIFGTGCNAAYMEvvsnipKLEHDDIPPDSP--MAINCEYGAF- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 254 DDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKN 333
Cdd:cd24087  233 DNEHLVLPRTKYDVIIDEESPRPGQQAFEKMIAGYYLGEILRLVLLDLYDEGFLFKGQDTSKLEKPYVMDTSFLSRIEED 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 334 K-EGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRlRDNKGtprlrTTVGVDGSLYKTHPQY 411
Cdd:cd24087  313 PfENLEDTDDLFQHfFGLETTVPERKFIRRLAELIGTRAARLSACGIAAICKK-RGYKT-----CHVAADGSVYNKYPGF 386

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 188497750 412 SRRFHKTLRRL----VPDSDVRFLLSESGSGKGAAMVTAVA 448
Cdd:cd24087  387 KERAAQALKDIfgwdGEDDPIKTVPAEDGSGVGAAIIAALT 427
Hexokinase_2 pfam03727
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 213-447 1.93e-100

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam00349. Some members of the family have two copies of each of these domains.


Pssm-ID: 461028  Cd Length: 236  Bit Score: 312.89  E-value: 1.93e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  213 EVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMY 289
Cdd:pfam03727   1 RIGLILGTGTNAAYVEKVSNIPKLEGKlpkSGEMIINTEWGAFGDNGLLPLPRTEYDKELDAESPNPGFQPFEKMISGMY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  290 LGELVRLILVKMAKEGLLFEGRiTPELLTRGKFNTSDVSAIEK-NKEGLHNAKEILTR-LGVE-PSDDDCVSVQHVCTIV 366
Cdd:pfam03727  81 LGELVRLVLLDLAEEGLLFKGQ-SEKLKTPYSLDTSFLSAIESdPSEDLETTREILEElLGIEtVTEEDRKIVRRICEAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  367 SFRSANLVAATLGAILNRLRDNKgtprlRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSD-VRFLLSESGSGKGAAMVT 445
Cdd:pfam03727 160 STRAARLVAAGIAAILKKIGRDK-----KVTVGVDGSVYEKYPGFRERLQEALRELLGPGDkVVLVLAEDGSGVGAALIA 234


                  ..
gi 188497750  446 AV 447
Cdd:pfam03727 235 AV 236
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 1-448 3.67e-100

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 319.60  E-value: 3.67e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750   1 MAKRALHDFIDKYlyAMRLSDETLIDIMTRFRKEMKNGLSRDfnpTATVKMLPTFVrSIPDGS-EKGDFIALDLGGSSFR 79
Cdd:COG5026    1 MKKLLVDAFLKRH--GFDLSSIDLEEIAAKFQEEMEKGLEGK---KSSLKMLPSYL-GLPTGVkETGPVIALDAGGTNFR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  80 ILRVQVNheKNQNVHMESEVY----DTPENIvhgSGSQLFDHVAECLGDFmekrkiKDKKLPVGFTFSFPCQQSKIDEAI 155
Cdd:COG5026   75 VALVRFD--GEGTFEIENFKSfplpGTSSEI---TAEEFFDFIADYIEPL------LDESYKLGFCFSFPAEQLPDKDGR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 156 LITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQ----HCEVGLIIGTGTNACYMEELR 231
Cdd:COG5026  144 LIQWTKEIKTPGVEGKNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPddgySGYIGSILGTGHNTCYLEPNA 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 232 HIDLVEGDEGRMCINTEWGAFgdDGSLediRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGlLFEGR 311
Cdd:COG5026  224 PIGKLPAYEGPMIINMESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 312 ITPELLTRGKFNTSDVSAIEKNKEGlhnAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLrDNKGT 391
Cdd:COG5026  298 FSEVFETPYSLTTVDMSRFLADPSD---EKEILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHL-GPGKT 373

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 392 PRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSD---VRFLLSESGSGKGAAMVTAVA 448
Cdd:COG5026  374 PLKPHCIAIDGSTYEKMPGLAEKIEYALQEYLLGEKgryVEFVLVENASLLGAAIAAALN 433
ASKHA_NBD_GLK1-2_fungi cd24088
nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 ...
 21-444 3.42e-98

nucleotide-binding domain (NBD) of hexokinase isozymes glucokinase-1 (GLK-1) and glucokinase-2 (GLK-2) from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (also known as glucokinase-1, EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. It is a putative glucokinase that functions in phosphorylation of aldohexoses and glucose uptake. It is involved in sporulation and required for the full activation of the early meiotic inducer IME1. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to glucokinase-1 and glucokinase-2.


Pssm-ID: 466938 [Multi-domain]  Cd Length: 445  Bit Score: 314.72  E-value: 3.42e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  21 DETLIDIMTRFRKEMKNGLSrdfNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheKNQNVHMESEVY 100
Cdd:cd24088    1 DEKLDKLTAEFQRQMEKGLA---KHGKGMAMIPTYVTGVPDGTETGTYLALDLGGTNFRVCSVELH--GDGTFSLRQEKS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 101 DTPENIVHGSGSQ-LFDHVAECLGDFMEK-------RKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGAD 172
Cdd:cd24088   76 KIPDELKTGVTAKdLFDYLAKSVEAFLTKhhgdsfaAGKDDDRLKLGFTFSFPVDQTAINSGTLIRWTKGFDIADAVGKD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 173 VVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCE---VGLIIGTGTNACYMEELRHI---DLVEGDE---GRM 243
Cdd:cd24088  156 VVKLLQDELDRQG-IPVKVVALVNDTVGTLLARSYTSPEISgavLGAIFGTGTNGAYLEDLEKIkklDDSSRVGkgkTHM 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 244 CINTEWGAFGDDGSLEDIrTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLL---FEGRITPELLTRG 320
Cdd:cd24088  235 VINTEWGSFDNELKVLPT-TPYDNKLDQKSSNPGFQMFEKRISGMYLGEILRNILVDLHKQGLFliqYNDKSPSALNTPY 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 321 KFNTSDVSAIEKNKE-GLHNAKEILTR-LGVE-PSDDDCVSVQHVCTIVSFRSANLVAATLGAIL---NRLRDNKGTPrl 394
Cdd:cd24088  314 GLDTAVLSAIEIDSEaELRATRKVLLDdLGLPaPSLEDAEAVRKISRAIGRRAARLSAVAIAAILiktGALNKSYDGE-- 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 188497750 395 rTTVGVDGSLYKTHPQYSRRFHKTLRRLVP----DSDVRFLLSESGSGKGAAMV 444
Cdd:cd24088  392 -INIGVDGSVIEFYPGFESMLREALRLLLIgaegEKRIKIGIAKDGSGVGAALC 444
PLN02914 PLN02914
hexokinase
 16-446 1.24e-97

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 314.90  E-value: 1.24e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  16 AMRLSDETLIDIMTRFRKE------------------MKNGLSRDfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSS 77
Cdd:PLN02914  29 AVRSNAVSVAPILTKLQKDcatplpvlrhvadamaadMRAGLAVD--GGGDLKMILSYVDSLPSGNEKGLFYALDLGGTN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  78 FRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIK-----DKKLPVGFTFSFPCQQSKID 152
Cdd:PLN02914 107 FRVLRVQLGGKDERVIATEFEQVSIPQELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSID 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 153 EAILITWTKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRH 232
Cdd:PLN02914 187 SGILMKWTKGFAVSGTAGKDVVACLNEAMERQG-LDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDA 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 233 IDLVEGDE---GRMCINTEWGAFGDDGSLedirTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFe 309
Cdd:PLN02914 266 IPKLQGQKsssGRTIINTEWGAFSDGLPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLF- 340

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 310 GRITPE-LLTRGKFNTSDVSAIEK-NKEGLHNAKEILTR-LGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL- 385
Cdd:PLN02914 341 GHFVPEkLSTPFALRTPHLCAMQQdNSDDLQAVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMe 420

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188497750 386 RDNKGT-PRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPD---SDVRFLLSESGSGKGAAMVTA 446
Cdd:PLN02914 421 EDSKGMiFGKRTVVAMDGGLYEKYPQYRRYMQDAVTELLGLelsKNIAIEHTKDGSGIGAALLAA 485
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 457-655 1.67e-94

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.


Pssm-ID: 459774 [Multi-domain]  Cd Length: 197  Bit Score: 295.57  E-value: 1.67e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  457 QIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQThnNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsG 536
Cdd:pfam00349   1 ELEELLKQFALSDEKLKEIVDRFVEEMEKGLAKEG--SSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVEL--G 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  537 KKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIK---GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKA 613
Cdd:pfam00349  77 GDGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEdfeEKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 188497750  614 TDCVGHDVVTLLRDAIKRREEfDLDVVAVVNDTVGTMMTCAY 655
Cdd:pfam00349 157 PGVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
COG5026 COG5026
Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway ...
 464-891 4.13e-92

Hexokinase [Carbohydrate transport and metabolism]; Hexokinase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 444044 [Multi-domain]  Cd Length: 434  Bit Score: 298.02  E-value: 4.13e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 464 HFHLTKDMLLEVKKRMRAEMELGLRkqtHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIrsGKKRTVEM 543
Cdd:COG5026   14 GFDLSSIDLEEIAAKFQEEMEKGLE---GKKSSLKMLPSYLGLPTGVKETGPVIALDAGGTNFRVALVRF--DGEGTFEI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 544 HNKIyAIPieiMQGTG-----EELFDHIVSCISDFLDYmgikgpRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVG 618
Cdd:COG5026   89 ENFK-SFP---LPGTSseitaEEFFDFIADYIEPLLDE------SYKLGFCFSFPAEQLPDKDGRLIQWTKEIKTPGVEG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 619 HDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTC----EVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCIN 694
Cdd:COG5026  159 KNIGELLEAALARKGLDNVKPVAILNDTVATLLAGAYADPDDgysgYIGSILGTGHNTCYLEPNAPIGKLPAYEGPMIIN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 695 MEWGAFgdNGCLddiRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGfLFRGQISETLKTRGIFETKF 774
Cdd:COG5026  239 MESGNF--NKLP---RTKIDEILDQQSEKPGEQLLEKMVSGRYLGELCRLTLREAAAEG-LFSPGFSEVFETPYSLTTVD 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 775 LSQI---ESDRLallqvrAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRlNVTVGVDGT 851
Cdd:COG5026  313 MSRFladPSDEK------EILSQCLEAGSEEDREILREIADAIVERAARLVAATLAGILLHLGPGKTPLK-PHCIAIDGS 385

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 188497750 852 LYKLHPHF-SRIMHQTVKELSPKCN--VSFLLSEDGSGKGAAL 891
Cdd:COG5026  386 TYEKMPGLaEKIEYALQEYLLGEKGryVEFVLVENASLLGAAI 428
PLN02914 PLN02914
hexokinase
 472-894 4.37e-91

hexokinase


Pssm-ID: 178502 [Multi-domain]  Cd Length: 490  Bit Score: 297.57  E-value: 4.37e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 472 LLEVKKRMRAEMELGLRKQTHNNavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIP 551
Cdd:PLN02914  55 LRHVADAMAADMRAGLAVDGGGD--LKMILSYVDSLPSGNEKGLFYALDLGGTNFRVLRVQLGGKDERVIATEFEQVSIP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 552 IEIMQGTGEELFDHIVSCISDFLDYMGIK-----GPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 626
Cdd:PLN02914 133 QELMFGTSEELFDFIASGLANFVAKEGGKfhlpeGRKREIGFTFSFPVKQTSIDSGILMKWTKGFAVSGTAGKDVVACLN 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 627 DAIKrREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQ---GQMCINMEWGAFGDN 703
Cdd:PLN02914 213 EAME-RQGLDMRVSALVNDTVGTLAGARYWDDDVMVAVILGTGTNACYVERTDAIPKLQGQKsssGRTIINTEWGAFSDG 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 704 GCLddirTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 783
Cdd:PLN02914 292 LPL----TEFDREMDAASINPGEQIFEKTISGMYLGEIVRRVLLKMAETSDLFGHFVPEKLSTPFALRTPHLCAMQQDNS 367

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 784 ALLQ-VRAILQQ-LGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENR---GLDRLNVtVGVDGTLYKLHPH 858
Cdd:PLN02914 368 DDLQaVGSILYDvLGVEASLSARRRVVEVCDTIVKRGGRLAGAGIVGILEKMEEDSkgmIFGKRTV-VAMDGGLYEKYPQ 446

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 188497750 859 FSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 894
Cdd:PLN02914 447 YRRYMQDAVTELlglELSKNIAIEHTKDGSGIGAALLAA 485
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 10-207 5.35e-83

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.


Pssm-ID: 459774 [Multi-domain]  Cd Length: 197  Bit Score: 265.14  E-value: 5.35e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750   10 IDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDfnPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNheK 89
Cdd:pfam00349   2 LEELLKQFALSDEKLKEIVDRFVEEMEKGLAKE--GSSSLKMLPTYVTSLPTGTEKGTFLALDLGGTNFRVCLVELG--G 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750   90 NQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKD---KKLPVGFTFSFPCQQSKIDEAILITWTKRFKAS 166
Cdd:pfam00349  78 DGKFEITQEKYKIPEELMTGTGEELFDFIADCIAEFLKEHGLEDfeeKELPLGFTFSFPVEQTSLDSGTLIRWTKGFDIP 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 188497750  167 GVEGADVVKLLNKAIKKRGDyDANIVAVVNDTVGTMMTCGY 207
Cdd:pfam00349 158 GVVGKDVVQLLQEALERRGL-PVKVVALVNDTVGTLMAGAY 197
PLN02405 PLN02405
hexokinase
 472-894 1.08e-79

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 267.08  E-value: 1.08e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 472 LLEVKKRMRAEMELGLrkQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIP 551
Cdd:PLN02405  55 LRQVADAMTVEMHAGL--ASEGGSKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIP 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 552 IEIMQGTGEELFDHIVSCISDFL-----DYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLR 626
Cdd:PLN02405 133 PHLMTGSSDALFDFIAAALAKFVategeDFHLPPGRQRELGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELT 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 627 DAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGD---QGQMCINMEWGAFGDN 703
Cdd:PLN02405 213 KAMERV-GLDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFRSS 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 704 GClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 783
Cdd:PLN02405 292 HL---PLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMHHDTS 368

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 784 ALLQV-----RAILQQlgLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIREN--RGLDRLNVTVGVDGTLYKLH 856
Cdd:PLN02405 369 PDLKVvgsklKDILEI--PNTSLKMRKVVVELCNIVATRGARLSAAGIYGILKKLGRDtvKDGEKQKSVIAMDGGLFEHY 446

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 188497750 857 PHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 894
Cdd:PLN02405 447 TEFSKCMESTLKELlgeEVSESIEVEHSNDGSGIGAALLAA 487
PLN02362 PLN02362
hexokinase
 472-894 2.37e-79

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 266.36  E-value: 2.37e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 472 LLEVKKRMRAEMELGLrkQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLlvKIRSGKKRT------VEMHn 545
Cdd:PLN02362  55 LRQVVDAMAVEMHAGL--ASEGGSKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVL--RVQLGGQRSsilsqdVERH- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 546 kiyAIPIEIMQGTGEELFDHIVSCISDFLDYMG-----IKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHD 620
Cdd:PLN02362 130 ---PIPQHLMNSTSEVLFDFIASSLKQFVEKEEngsefSQVRRRELGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKD 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 621 VVTLLRDAIKRReEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEW 697
Cdd:PLN02362 207 VAECLQGALNRR-GLDMRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEW 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 698 GAFGDNGClddIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFrGQISETLKTRGIFETKFLSQ 777
Cdd:PLN02362 286 GNFWSSHL---PRTSYDIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAA 361

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 778 I-ESDRLALLQVRAILQQ-LGLNST-CDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKI-------------RENRGLDR 841
Cdd:PLN02362 362 MhEDDSPELQEVARILKEtLGISEVpLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgrdgsggitsgrsRSDIQIMR 441

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 188497750 842 LNVtVGVDGTLYKLHPHFSRIMHQTVKEL---SPKCNVSFLLSEDGSGKGAALITA 894
Cdd:PLN02362 442 RTV-VAVEGGLYTNYTMFREYLHEALNEIlgeDVAQHVILKATEDGSGIGSALLAA 496
PLN02405 PLN02405
hexokinase
 26-446 1.14e-74

hexokinase


Pssm-ID: 215226 [Multi-domain]  Cd Length: 497  Bit Score: 253.22  E-value: 1.14e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  26 DIMTrfrKEMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPEN 105
Cdd:PLN02405  60 DAMT---VEMHAGLASEGG--SKLKMLISYVDNLPSGDEKGLFYALDLGGTNFRVLRVLLGGKDGRVVKQEFEEVSIPPH 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 106 IVHGSGSQLFDHVAECLGDFMEKRKiKDKKLP------VGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNK 179
Cdd:PLN02405 135 LMTGSSDALFDFIAAALAKFVATEG-EDFHLPpgrqreLGFTFSFPVKQTSISSGTLIKWTKGFSIDDAVGQDVVGELTK 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 180 AIKKRGdYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGD---EGRMCINTEWGAFGddg 256
Cdd:PLN02405 214 AMERVG-LDMRVSALVNDTIGTLAGGRYYNPDVVAAVILGTGTNAAYVERAQAIPKWHGLlpkSGEMVINMEWGNFR--- 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 257 SLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEknkeg 336
Cdd:PLN02405 290 SSHLPLTEYDHALDVESLNPGEQIFEKIISGMYLGEILRRVLLKMAEEAAFFGDTVPPKLKIPFILRTPDMSAMH----- 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 337 lHNAKEILTRLGVEPSDDDCVS---------VQHVCTIVSFRSANLVAATLGAILNRL-RDN-KGTPRLRTTVGVDGSLY 405
Cdd:PLN02405 365 -HDTSPDLKVVGSKLKDILEIPntslkmrkvVVELCNIVATRGARLSAAGIYGILKKLgRDTvKDGEKQKSVIAMDGGLF 443

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 188497750 406 KTHPQYSRRFHKTLRRLVPDS---DVRFLLSESGSGKGAAMVTA 446
Cdd:PLN02405 444 EHYTEFSKCMESTLKELLGEEvseSIEVEHSNDGSGIGAALLAA 487
PLN02362 PLN02362
hexokinase
 34-446 2.42e-71

hexokinase


Pssm-ID: 215206 [Multi-domain]  Cd Length: 509  Bit Score: 244.79  E-value: 2.42e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  34 EMKNGLSRDFNptATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQ 113
Cdd:PLN02362  65 EMHAGLASEGG--SKLKMLLTFVDDLPTGSEIGTYYALDLGGTNFRVLRVQLGGQRSSILSQDVERHPIPQHLMNSTSEV 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 114 LFDHVAECLGDFMEKRKIKDKKLPV-----GFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGdYD 188
Cdd:PLN02362 143 LFDFIASSLKQFVEKEENGSEFSQVrrrelGFTFSFPVKQTSISSGILIKWTKGFAISDMVGKDVAECLQGALNRRG-LD 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 189 ANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFgddGSLEDIRTEF 265
Cdd:PLN02362 222 MRVAALVNDTVGTLALGHYHDPDTVAAVIIGTGTNACYLERTDAIIKCQGlltTSGSMVVNMEWGNF---WSSHLPRTSY 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 266 DREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFeGRITPELLTRGKFNTSDVSAI-EKNKEGLHNAKEIL 344
Cdd:PLN02362 299 DIDLDAESPNPNDQGFEKMISGMYLGDIVRRVILRMSQESDIF-GPVSSRLSTPFVLRTPSVAAMhEDDSPELQEVARIL 377

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 345 T-RLGV-EPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRL-RDNKG-----------TPRLRTTVGVDGSLYKTHPQ 410
Cdd:PLN02362 378 KeTLGIsEVPLKVRKLVVKICDVVTRRAARLAAAGIVGILKKIgRDGSGgitsgrsrsdiQIMRRTVVAVEGGLYTNYTM 457

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 188497750 411 YSRRFHKTLRRLVPDSDVRFLL---SESGSGKGAAMVTA 446
Cdd:PLN02362 458 FREYLHEALNEILGEDVAQHVIlkaTEDGSGIGSALLAA 496
PLN02596 PLN02596
hexokinase-like
 46-446 7.15e-50

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 183.92  E-value: 7.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750  46 TATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQV--NHEKNQNVHMEsEVyDTPENIVHGSGSQLFDHVAECLG 123
Cdd:PLN02596  76 TTTLNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLggKNEPISDLYRE-EI-SIPSNVLNGTSQELFDYIALELA 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 124 DFMEKRKIKDKKLP-----VGFTFSFPCQQSKIDEAILITWtKRFKASGVEGADVVKLLNKAIKKRGdYDANIVAVVNDT 198
Cdd:PLN02596 154 KFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDINRALEKHG-LKIRVFALVDDT 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 199 VGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEG---DEGRMCINTEWGAFGddgSLEDIRTEFDREIDRGSLN 275
Cdd:PLN02596 232 IGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNFN---SCHLPITEFDASLDAESSN 308

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 276 PGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSA----IEKNKEGLHNA-KEILTRLGVE 350
Cdd:PLN02596 309 PGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAmhqdTSEDHEVVNEKlKEIFGITDST 388

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 351 PSDDDCVSvqHVCTIVSFRSANLVAATLGAILNRLR--DNKgtprlRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPD--S 426
Cdd:PLN02596 389 PMAREVVA--EVCDIVAERGARLAGAGIVGIIKKLGriENK-----KSVVTVEGGLYEHYRVFRNYLHSSVWEMLGSelS 461

                        410       420
                 ....*....|....*....|.
gi 188497750 427 D-VRFLLSESGSGKGAAMVTA 446
Cdd:PLN02596 462 DnVVIEHSHGGSGAGALFLAA 482
PLN02596 PLN02596
hexokinase-like
 472-896 1.81e-48

hexokinase-like


Pssm-ID: 178206 [Multi-domain]  Cd Length: 490  Bit Score: 179.69  E-value: 1.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 472 LLEVKKRMRAEMELGLRKQTHNNavVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIP 551
Cdd:PLN02596  56 LWEVADALVSDMTASLTAEETTT--LNMLVSYVASLPSGDEKGLYYGLNLRGSNFLLLRARLGGKNEPISDLYREEISIP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 552 IEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMP-----LGFTFSFPCQQTSLDAGILITWtKGFKATDCVGHDVVTLLR 626
Cdd:PLN02596 134 SNVLNGTSQELFDYIALELAKFVAEHPGDEADTPervkkLGFTVSYPVDQAAASSGSAIKW-KSFSADDTVGKALVNDIN 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 627 DAIKRrEEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEG---DQGQMCINMEWGAFgdN 703
Cdd:PLN02596 213 RALEK-HGLKIRVFALVDDTIGNLAGGRYYNKDTVAAVTLGMGTNAAYVEPAQAIPKWQSpspESQEIVISTEWGNF--N 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 704 GCLDDIrTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRL 783
Cdd:PLN02596 290 SCHLPI-TEFDASLDAESSNPGSRIFEKLTSGMYLGEIVRRVLLKMAEETALFGDTLPPKLTTPYLLRSPDMAAMHQDTS 368

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188497750 784 ALLQV--RAILQQLGL-NSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIreNRGLDRLNVtVGVDGTLYKLHPHFS 860
Cdd:PLN02596 369 EDHEVvnEKLKEIFGItDSTPMAREVVAEVCDIVAERGARLAGAGIVGIIKKL--GRIENKKSV-VTVEGGLYEHYRVFR 445

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 188497750 861 RIMHQTV-----KELSPkcNVSFLLSEDGSGKGAALITAVG 896
Cdd:PLN02596 446 NYLHSSVwemlgSELSD--NVVIEHSHGGSGAGALFLAACQ 484
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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