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Conserved domains on  [gi|1039768924|ref|XP_017175919|]
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FGGY carbohydrate kinase domain-containing protein isoform X8 [Mus musculus]

Protein Classification

FGGY-family carbohydrate kinase( domain architecture ID 10167359)

FGGY-family carbohydrate kinase catalyzes the ATP-dependent phosphorylation of a carbohydrate substrate to produce phosphorylated sugar and ADP; similar to Homo sapiens FGGY carbohydrate kinase domain-containing protein and Saccharomyces cerevisiae D-ribulokinase YDR109C

CATH:  3.30.420.40
EC:  2.7.1.-
Gene Ontology:  GO:0016310|GO:0019200|GO:0005524
SCOP:  3000092

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
12-433 0e+00

nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.


:

Pssm-ID: 466800 [Multi-domain]  Cd Length: 540  Bit Score: 787.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 89
Cdd:cd07782     1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 169
Cdd:cd07782    81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 170 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:cd07782   160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07782   240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 403
Cdd:cd07782   318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
                         410       420       430
                  ....*....|....*....|....*....|
gi 1039768924 404 TLKGMVTGLTLSQDLDDLAILYLATVQAIA 433
Cdd:cd07782   398 TLRGMISGLTLDTSLDDLALLYLATLQALA 427
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
12-433 0e+00

nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.


Pssm-ID: 466800 [Multi-domain]  Cd Length: 540  Bit Score: 787.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 89
Cdd:cd07782     1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 169
Cdd:cd07782    81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 170 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:cd07782   160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07782   240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 403
Cdd:cd07782   318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
                         410       420       430
                  ....*....|....*....|....*....|
gi 1039768924 404 TLKGMVTGLTLSQDLDDLAILYLATVQAIA 433
Cdd:cd07782   398 TLRGMISGLTLDTSLDDLALLYLATLQALA 427
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
12-433 0e+00

FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.


Pssm-ID: 273552 [Multi-domain]  Cd Length: 541  Bit Score: 544.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDATCS 89
Cdd:TIGR01315   1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 169
Cdd:TIGR01315  81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 170 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 401
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1039768924 402 DLTLKGMVTGLTLSQDLDDLAILYLATVQAIA 433
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIA 427
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
10-433 8.77e-159

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 462.28  E-value: 8.77e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  10 SRYYVGIDVGTGSVRAALVDQR-GLLLAFAEQPIKKWEP---------QFnhhEQSSEDIWAACCLVTKEVVQ--GIDAH 77
Cdd:COG1069     1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  78 RIRGLGFDAT-CSLVVLDKEFHPLPVNHE--GDSSRNVIMWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPK 150
Cdd:COG1069    78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 151 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGN 226
Cdd:COG1069   158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 227 LVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKD 306
Cdd:COG1069   233 EIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPE 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 307 PVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVD 386
Cdd:COG1069   299 ERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESG 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1039768924 387 LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIA 433
Cdd:COG1069   373 LHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATA 416
PRK04123 PRK04123
ribulokinase; Provisional
12-433 1.19e-56

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 198.15  E-value: 1.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKW---------EPQFNHHEQSSEDIWAAcclVTKEVVQ--GIDAHRI 79
Cdd:PRK04123    4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPAAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  80 RGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKL 151
Cdd:PRK04123   81 VGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 152 LWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnys 222
Cdd:PRK04123  161 LHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 223 KIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAgglGVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMG 302
Cdd:PRK04123  237 KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHM---GAVGAGAEPGTLV----------KVM-GTSTCDIL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 303 ISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA- 377
Cdd:PRK04123  302 LADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAa 370
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 378 -QPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIA 433
Cdd:PRK04123  371 kQPPgehGLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPD---IYRALIEATA 422
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
290-434 1.61e-31

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 120.51  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 290 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQakATARCQSIYAYLN 368
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768924 369 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQdldDLAILYLATVQAIAA 434
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPT---TLAHLYRAILESLAL 132
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
12-433 0e+00

nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.


Pssm-ID: 466800 [Multi-domain]  Cd Length: 540  Bit Score: 787.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 89
Cdd:cd07782     1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 169
Cdd:cd07782    81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 170 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:cd07782   160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07782   240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 403
Cdd:cd07782   318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
                         410       420       430
                  ....*....|....*....|....*....|
gi 1039768924 404 TLKGMVTGLTLSQDLDDLAILYLATVQAIA 433
Cdd:cd07782   398 TLRGMISGLTLDTSLDDLALLYLATLQALA 427
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
12-433 0e+00

FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.


Pssm-ID: 273552 [Multi-domain]  Cd Length: 541  Bit Score: 544.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDATCS 89
Cdd:TIGR01315   1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 169
Cdd:TIGR01315  81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 170 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 401
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1039768924 402 DLTLKGMVTGLTLSQDLDDLAILYLATVQAIA 433
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIA 427
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
10-433 8.77e-159

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 462.28  E-value: 8.77e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  10 SRYYVGIDVGTGSVRAALVDQR-GLLLAFAEQPIKKWEP---------QFnhhEQSSEDIWAACCLVTKEVVQ--GIDAH 77
Cdd:COG1069     1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  78 RIRGLGFDAT-CSLVVLDKEFHPLPVNHE--GDSSRNVIMWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPK 150
Cdd:COG1069    78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 151 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGN 226
Cdd:COG1069   158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 227 LVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKD 306
Cdd:COG1069   233 EIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPE 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 307 PVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVD 386
Cdd:COG1069   299 ERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESG 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1039768924 387 LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIA 433
Cdd:COG1069   373 LHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATA 416
ASKHA_NBD_FGGY_RBK-like cd07768
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ...
12-433 4.06e-123

nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466788 [Multi-domain]  Cd Length: 522  Bit Score: 370.80  E-value: 4.06e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE-PQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDAT 87
Cdd:cd07768     1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  88 CSLVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:cd07768    81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 167 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDLiDDNYSKIGNLVLLPGAALGIGLtPEAAR 245
Cdd:cd07768   160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGhgltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07768   238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQaKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTL 405
Cdd:cd07768   306 SVYEAGQSATGKLIEHLFESHPCARKFD-EALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRL 381
                         410       420
                  ....*....|....*....|....*...
gi 1039768924 406 KGMVTGLTLSQDLDDLAILYLATVQAIA 433
Cdd:cd07768   382 KGSFIGESLDTSMLNLTYKYIAILEALA 409
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
12-433 9.39e-108

nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466799 [Multi-domain]  Cd Length: 504  Bit Score: 330.65  E-value: 9.39e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--PQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA 86
Cdd:cd07781     1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  87 TCS-LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRV----LQYVGGVMSVEMQAPKLLWLKENLREI 161
Cdd:cd07781    81 TSStVVPVDEDGNPL---------APAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 162 cWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDLidDNYSKIGNLVLLPGAALGiGLT 240
Cdd:cd07781   152 -YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGLL--KLREKLPGEVVPVGEPAG-TLT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 241 PEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSA 320
Cdd:cd07781   228 AEAAERLGLPAGIPVAQGGIDAHMG---AIGAGVVEPG----------TLALIMGTSTCHLMVSPKPVDIPGICGPVPDA 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 321 MVPGFWLNEGGQSVTGKLIDhmvqghpAFPELQAKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNR 397
Cdd:cd07781   295 VVPGLYGLEAGQSAVGDIFA-------WFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNR 359
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1039768924 398 SPLADLTLKGMVTGLTLSQdldDLAILYLATVQAIA 433
Cdd:cd07781   360 TPLVDPRLRGAIVGLTLGT---TPAHIYRALLEATA 392
ASKHA_NBD_FGGY_MPA43-like cd07778
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ...
13-433 2.23e-75

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466797 [Multi-domain]  Cd Length: 544  Bit Score: 247.70  E-value: 2.23e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  13 YVGIDVGTGSVRAALVDQRGLLLAFAEQPI--KKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATCSL 90
Cdd:cd07778     2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  91 VVLDKE-----FHPLPVNHE-GDSSRNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICW 163
Cdd:cd07778    82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 164 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDLIDDNYSKIGNLVL 229
Cdd:cd07778   162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNVGNTFKEAPP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 230 LPGAALGIG-LTPEAARELGLPSGIAVAASLIDAHAGGLGVIgadvrghgltCEGQPVTSRLAVICGTSSCHMGISKDPV 308
Cdd:cd07778   233 LPYAGIPIGkVNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQ 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 309 --FVPGVWGPyYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATarcqSIYAYLNSHLDLI--KKAQPVGFLT 384
Cdd:cd07778   303 vgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLT 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1039768924 385 VDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIA 433
Cdd:cd07778   378 RHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLA 426
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
11-436 2.58e-63

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 214.31  E-value: 2.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  11 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT- 87
Cdd:COG1070     1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  88 CSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 165
Cdd:COG1070    81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 166 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGLEDLIddnyskignL--VLLPGAALGiG 238
Cdd:COG1070   151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIDREL---------LpeLVPPGEVAG-T 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 239 LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYY 318
Cdd:COG1070   217 LTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTF 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 319 SAMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKAtarcQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDF 393
Cdd:COG1070   284 CHAVPGRWLPMGATNNGGSALRWFRD------LFADGE----LDDYEELN---ALAAEV-PPGadgllFL-------PYL 342
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1039768924 394 HGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAACL 436
Cdd:COG1070   343 SGERTPHWDPNARGAFFGLTLSHTRAH---LARAVLEGVAFAL 382
PRK04123 PRK04123
ribulokinase; Provisional
12-433 1.19e-56

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 198.15  E-value: 1.19e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKW---------EPQFNHHEQSSEDIWAAcclVTKEVVQ--GIDAHRI 79
Cdd:PRK04123    4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPAAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  80 RGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKL 151
Cdd:PRK04123   81 VGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 152 LWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnys 222
Cdd:PRK04123  161 LHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD--- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 223 KIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAgglGVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMG 302
Cdd:PRK04123  237 KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHM---GAVGAGAEPGTLV----------KVM-GTSTCDIL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 303 ISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA- 377
Cdd:PRK04123  302 LADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAa 370
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 378 -QPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIA 433
Cdd:PRK04123  371 kQPPgehGLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPD---IYRALIEATA 422
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
12-422 7.89e-54

nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466807 [Multi-domain]  Cd Length: 485  Bit Score: 188.88  E-value: 7.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07805     1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQY---VGGVMSVEMQAPKLLWLKENLREIcWDK 165
Cdd:cd07805    81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEI-YAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 166 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLE-DLIDDnyskignlvLLPGAALgIG-LTPE 242
Cdd:cd07805   151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDpDKLPE---------LVPSTEV-VGeLTPE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 243 AARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrlAVIC-GTSS---CHmgiSKDPVFVPGvwGPYY 318
Cdd:cd07805   221 AAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGD-------------AHIYlGTSGwvaAH---VPKPKTDPD--HGIF 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 319 S--AMVPGFWLNEGGQSVTGKLIDHMVqghpafpELQAKATARCQSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPD 392
Cdd:cd07805   282 TlaSADPGRYLLAAEQETAGGALEWAR-------DNLGGDEDLGADDYELLD---ELAAEAPPgsngLLFL-------PW 344
                         410       420       430
                  ....*....|....*....|....*....|
gi 1039768924 393 FHGNRSPLADLTLKGMVTGLTLSQDLDDLA 422
Cdd:cd07805   345 LNGERSPVEDPNARGAFIGLSLEHTRADLA 374
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
12-433 3.13e-49

nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466801 [Multi-domain]  Cd Length: 429  Bit Score: 175.10  E-value: 3.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 90
Cdd:cd07783     1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  91 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 170
Cdd:cd07783    81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 171 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGL-EDLIddnyskigNLVLLPGAALGIgLTPEAARELG 248
Cdd:cd07783   151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIpPDLL--------PRVVAPGTVIGT-LTAEAAEELG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 249 LPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFVPGvwGPYYSAMVP-GFWL 327
Cdd:cd07783   222 LPAGTPVVAGTTDSIAAFLAS-GAVRPGDAVT------------SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGdGYWL 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 328 NEGGQSVTGKLIDHMVQGHPaFPELQAKATARCQSiyaylnshldlikkaqpvgfltvDLHVWP-DFHGNRSPLADLTLK 406
Cdd:cd07783   287 VGGASNTGGAVLRWFFSDDE-LAELSAQADPPGPS-----------------------GLIYYPlPLRGERFPFWDPDAR 342
                         410       420
                  ....*....|....*....|....*..
gi 1039768924 407 GMVTGLTlsqdlDDLAILYLATVQAIA 433
Cdd:cd07783   343 GFLLPRP-----HDRAEFLRALLEGIA 364
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
12-422 1.90e-46

nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466808 [Multi-domain]  Cd Length: 482  Bit Score: 168.87  E-value: 1.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDA-TC 88
Cdd:cd07808     1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 167
Cdd:cd07808    81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 168 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdliddnyskIGNL--VLLPGAALG 236
Cdd:cd07808   151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD---------PSILppIVESTEIVG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 237 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPV----TSrlAVICGTSSCHMGISKDPVF--- 309
Cdd:cd07808   214 -TLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfp 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 310 --VPGVWgpYYSAMVPGF-----WLNE--GGQSVTGKLIDHMVQGHPAfpelqakatarcqsiyaylnshldlikKAQPV 380
Cdd:cd07808   283 haVPGKW--YAMGVTLSAglslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGL 333
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1039768924 381 GFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLA 422
Cdd:cd07808   334 LFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA 368
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
12-329 1.85e-45

nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466805 [Multi-domain]  Cd Length: 444  Bit Score: 165.42  E-value: 1.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07802     1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:cd07802    81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 167 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDLIDdnysKIGNLVllPGAALGIGL 239
Cdd:cd07802   151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEELKD----KLPPLV--PSTEIAGRV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 240 TPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGpYYS 319
Cdd:cd07802   218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
                         330
                  ....*....|
gi 1039768924 320 AMVPGFWLNE 329
Cdd:cd07802   284 HADPGLYLIV 293
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
12-424 1.93e-44

nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466806 [Multi-domain]  Cd Length: 451  Bit Score: 162.70  E-value: 1.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFA--EQPIKKwePQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGfdat 87
Cdd:cd07804     1 YLLGIDIGTTGTKGVLVDEDGKVLASAsiEHDLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIG---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  88 CS-----LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLRE 160
Cdd:cd07804    75 VSglvpaLVPVDENGKPL---------RPAILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 161 IcWDKAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGL-EDLIDDNYSkignlvllPG 232
Cdd:cd07804   146 V-FKKTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGIdPDLLPELVP--------ST 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 233 AALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPG 312
Cdd:cd07804   212 EIVG-EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPR 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 313 VWGPYYSamVPGFWLNEGGQSVTGKLIDHMVQGhpAFPELQAKATARCQSIYAYLNshldliKKAQ--PVGfltVD-LHV 389
Cdd:cd07804   278 LWLDYHD--IPGTYVLNGGMATSGSLLRWFRDE--FAGEEVEAEKSGGDSAYDLLD------EEAEkiPPG---SDgLIV 344
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1039768924 390 WPDFHGNRSPLADLTLKGMVTGLTLSQDLDDL--AIL 424
Cdd:cd07804   345 LPYFMGERTPIWDPDARGVIFGLTLSHTRAHLyrALL 381
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
12-441 2.19e-44

nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466787 [Multi-domain]  Cd Length: 392  Bit Score: 161.19  E-value: 2.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd00366     1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAvsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 168
Cdd:cd00366    81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 169 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGLEDliddnySKIGNLVlLPGAALGiGLTPEAARE 246
Cdd:cd00366   105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIPR------EKLPPIV-ESGEVVG-RVTPEAAEE 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 247 LGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVtsrlaVICGTSSCHMGISKDPVFVPGVWGPYYSAmVPGFW 326
Cdd:cd00366   176 TGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLW 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 327 LNEGGQSVTGKLIDHMvqghpafpelqAKATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLAD 402
Cdd:cd00366   242 LLEGAINTGGASLRWF-----------RDEFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIWD 303
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1039768924 403 LTLKGMVTGLTLSQDLDDL--AIL------YLATVQAIAACLWSCHK 441
Cdd:cd00366   304 PAARGVFFGLTLSHTRAHLirAVLegvayaLRDNLEILEELGVKIKE 350
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
12-433 6.79e-41

nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466793 [Multi-domain]  Cd Length: 443  Bit Score: 152.74  E-value: 6.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFdAT--CS 89
Cdd:cd07773     1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  90 LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 167
Cdd:cd07773    80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 168 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDLIDDNYSKIGNLVlLPGAALGIgLTPEAAR 245
Cdd:cd07773   150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDASLLPELV-PSGTVIGT-VTPEAAE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYS---AMV 322
Cdd:cd07773   221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 323 PGFWLNEGGQSvTGKLIDHMVQghpafpELQAKATARCQSIYAYLNShldlIKKAQPVGFLtvdlhvwPDFHGNRSPLAD 402
Cdd:cd07773   288 GGYYYLAGSLP-GGALLEWFRD------LFGGDESDLAAADELAEAA----PPGPTGLLFL-------PHLSGSGTPDFD 349
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1039768924 403 LTLKGMVTGLTLSQDLDDlaiLYLATVQAIA 433
Cdd:cd07773   350 PDARGAFLGLTLGTTRAD---LLRAILEGLA 377
L-ribulokinase TIGR01234
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ...
12-433 2.63e-40

ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]


Pssm-ID: 130301 [Multi-domain]  Cd Length: 536  Bit Score: 153.16  E-value: 2.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--------------PQFNHHEQSSEDIWAAcclVTKEVVQ--GI 74
Cdd:TIGR01234   2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  75 DAHRIRGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR----VLQYVGGVMSVEMQ 147
Cdd:TIGR01234  79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEFAENPHayFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 148 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDLIDDNYSK- 223
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 224 IGNLvllpGAALGiGLTPEAARELGLPSGIAVAASLIDAHaggLGVIGADVrghgltceGQPvtSRLAVICGTSSCHMGI 303
Cdd:TIGR01234 238 IWTA----GEPAG-TLTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 304 SKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQgHPAFPELQAKATARCQSiyayLNSHLDLIKKAQPV--- 380
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgeh 374
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039768924 381 GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIA 433
Cdd:TIGR01234 375 GLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATA 419
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
12-424 3.79e-37

nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466798 [Multi-domain]  Cd Length: 433  Bit Score: 142.27  E-value: 3.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07779     1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 168
Cdd:cd07779    81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 169 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDliddnySKIGNLVlLPGAALGiGLTPEAAREL 247
Cdd:cd07779   106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGIDR------DKLPELV-PPGTVIG-TLTKEAAEET 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 248 GLPSGIAVAASlidAHAGGLGVIGAdvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWL 327
Cdd:cd07779   178 GLPEGTPVVAG---GGDQQCAALGA-----GVLEPGT-----ASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 328 NEGGQSVTGKLIDHMVQghpAFPELQAKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKG 407
Cdd:cd07779   245 LEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARG 315
                         410
                  ....*....|....*....
gi 1039768924 408 MVTGLTLSQDLDDL--AIL 424
Cdd:cd07779   316 AFIGLTLSHTRAHLarAIL 334
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
12-442 8.93e-35

nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466790 [Multi-domain]  Cd Length: 478  Bit Score: 136.15  E-value: 8.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 90
Cdd:cd07770     1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  91 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRI--NETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 168
Cdd:cd07770    81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 169 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdliDDNYSKignlvLLPGAALGIGLTPEA 243
Cdd:cd07770   151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQLPE-----LVDPTEVLPGLKPEF 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 244 ARELGLPSGIAVAASLIDAHAGGLGViGADVRGhgltcegqpvtsRLAVICGTSschmG----ISKDPVFVP--GVWgPY 317
Cdd:cd07770   219 AERLGLLAGTPVVLGASDGALANLGS-GALDPG------------RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 318 YSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHPAFPELQAKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPD 392
Cdd:cd07770   281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PY 336
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039768924 393 FHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAACLWSCHKR 442
Cdd:cd07770   337 LAGERAPGWNPDARGAFFGLTLNHTRAD---ILRAVLEGVAFNLKSIYEA 383
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
290-434 1.61e-31

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 120.51  E-value: 1.61e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 290 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQakATARCQSIYAYLN 368
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768924 369 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQdldDLAILYLATVQAIAA 434
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPT---TLAHLYRAILESLAL 132
ASKHA_NBD_FGGY_BaEryA-like cd24121
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
12-422 6.54e-30

nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466971 [Multi-domain]  Cd Length: 452  Bit Score: 121.96  E-value: 6.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGID--AHRIRGLGFDAT-- 87
Cdd:cd24121     1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDvlPDRVAAIGVTGQgd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  88 -CSLVvlDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICwD 164
Cdd:cd24121    81 gTWLV--DEDGRPV---------RDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 165 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDLIDdnyskignlvLLPGAALGIG--- 238
Cdd:cd24121   149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH----------LLPPIRPGTEvig 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 239 -LTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMgiskdpVFVPGVW-GP 316
Cdd:cd24121   216 pLTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDACS------------ILGTTGVHE------VVVDEPDlEP 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 317 YYSAM-----VPGFWLNEGGqSVTGKL-IDHMVQghPAFPELQAKATARCQSIYAYLNSHLdlikKAQPVGFLTVDLHVW 390
Cdd:cd24121   277 EGVGYticlgVPGRWLRAMA-NMAGTPnLDWFLR--ELGEVLKEGAEPAGSDLFQDLEELA----ASSPPGAEGVLYHPY 349
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1039768924 391 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLA 422
Cdd:cd24121   350 LSPAGERAPFVNPNARAQFTGLSLEHTRADLL 381
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
12-367 8.26e-27

nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466804 [Multi-domain]  Cd Length: 448  Bit Score: 113.09  E-value: 8.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHH--EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgfdAT 87
Cdd:cd07798     1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  88 CS----LVVLDKEFHPL---PvNHegdssrnvimwlDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAP-KLLWLKENLR 159
Cdd:cd07798    78 TSqregIVFLDKDGRELyagP-NI------------DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRP 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 160 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDLIddnyskignL--VL 229
Cdd:cd07798   145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPPEI---------LpeIV 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 230 LPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrLAVICGTSSCHMGISKDPVF 309
Cdd:cd07798   208 PSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEPII 273
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039768924 310 VP--GVW-GPYysaMVPGFWLNEGGQSVTG----KLIDHMVQGHPA----FPELQAKATARCQSIYAYL 367
Cdd:cd07798   274 DPerRLWtGCH---LVPGKWVLESNAGVTGlnyqWLKELLYGDPEDsyevLEEEASEIPPGANGVLAFL 339
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
12-308 3.98e-26

nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466809 [Multi-domain]  Cd Length: 443  Bit Score: 110.72  E-value: 3.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPikkWEPQFNHH---EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD 85
Cdd:cd07809     1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAP---HENILIDPgwaEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGIS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  86 ATC-SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcW 163
Cdd:cd07809    78 GQMhGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-Y 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 164 DKAgHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDLIDDNYSKIGNlVLLPGAAL 235
Cdd:cd07809   148 ARI-AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLPE-VLPAGEVA 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039768924 236 GiGLTPEAARELGLPSGIAVAASLIDAHAG--GLGVIGadvrghgltcEGQPVTSrlaviCGTSSCHMGISKDPV 308
Cdd:cd07809   217 G-RLTPEGAEELGLPAGIPVAPGEGDNMTGalGTGVVN----------PGTVAVS-----LGTSGTAYGVSDKPV 275
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
12-268 8.16e-26

FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 105.88  E-value: 8.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATC- 88
Cdd:pfam00370   1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:pfam00370  81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 167 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdliDDNYSKignlvLLPGAALGIG 238
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP---RDHLPP-----LVESSEIYGE 215
                         250       260       270
                  ....*....|....*....|....*....|
gi 1039768924 239 LTPEAARELGLPSGIAVAASLIDAHAGGLG 268
Cdd:pfam00370 216 LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
12-270 4.31e-16

nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466794 [Multi-domain]  Cd Length: 492  Bit Score: 80.84  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKWEPQFNHHEQSSEDI-----WAACCLVTKEVVQ--GIDAHRIRGLgf 84
Cdd:cd07775     1 YLLALDAGTGSGRAVIFDLEGNQIAVAQ---REWRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  85 dATCS----LVVLDKEFHPLPVNHegdssrNVimwlDHRAVSQVHRINETKH---RVLQYVGGVMSVEMQAPKLLWLKEN 157
Cdd:cd07775    76 -STTSmregIVLYDNEGEEIWACA------NV----DARAAEEVSELKELYNtleEEVYRISGQTFALGAIPRLLWLKNN 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 158 LREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDLIDDNyskignlVLLPGAAL 235
Cdd:cd07775   145 RPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKADILPP-------VVESGTVI 215
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039768924 236 GIgLTPEAARELGLPSGIAVAASLIDAHAG--GLGVI 270
Cdd:cd07775   216 GK-VTKEAAEETGLKEGTPVVVGGGDVQLGclGLGVV 251
PRK15027 PRK15027
xylulokinase; Provisional
13-422 1.13e-15

xylulokinase; Provisional


Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 79.63  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  13 YVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC-----CLVTKEVVQGIDAHRIRGLGFDAT 87
Cdd:PRK15027    2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATdramkALGDQHSLQDVKALGIAGQMHGAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  88 cslvVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAG 167
Cdd:PRK15027   82 ----LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 168 HFfdLP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDLIDDNYSkignlVLLPGAALGIGLTPEAAR 245
Cdd:PRK15027  149 VL--LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 246 ELGLPSgIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVTSrlaviCGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:PRK15027  219 AWGMAT-VPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQR 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 326 WlneggqsvtgKLIDHMVQGHPAFpELQAKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTL 405
Cdd:PRK15027  285 W----------HLMSVMLSAASCL-DWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQA 345
                         410
                  ....*....|....*..
gi 1039768924 406 KGMVTGLTLSQDLDDLA 422
Cdd:PRK15027  346 KGVFFGLTHQHGPNELA 362
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
12-314 3.00e-12

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 68.88  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKW----EPQF-NHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgf 84
Cdd:PRK10939    4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  85 dATCSL----VVLDKEFHPLpvnhegdssrnvimW----LDHRAVSQV----HRINETKHRVLQYVGGVMSVEmQAPKLL 152
Cdd:PRK10939   79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVselkELHNNFEEEVYRCSGQTLALG-ALPRLL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 153 WLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGledLIDDNYSKi 224
Cdd:PRK10939  143 WLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAG---LRADILPP- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 225 gnlVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGT-------- 296
Cdd:PRK10939  211 ---VKETGTVLG-HVTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnl 273
                         330       340
                  ....*....|....*....|..
gi 1039768924 297 ----SSCHMGISKDPVFVPGVW 314
Cdd:PRK10939  274 papvTDPNMNIRINPHVIPGMV 295
ASKHA_NBD_FGGY_GK cd07769
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ...
12-158 2.70e-10

nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466789 [Multi-domain]  Cd Length: 486  Bit Score: 62.48  E-value: 2.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdaTC- 88
Cdd:cd07769     1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039768924  89 --SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKENL 158
Cdd:cd07769    79 reTTVVWDK--------KTGKPLYNAIVWQDRRTADICEELKAKGLeeRIREKTGLPLDPYFSATKIKWILDNV 144
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
12-132 1.63e-09

Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases


Pssm-ID: 198361 [Multi-domain]  Cd Length: 486  Bit Score: 60.20  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD---A 86
Cdd:cd07786     1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAkaGIRASDIAAIGITnqrE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039768924  87 TCslVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHRINETKH 132
Cdd:cd07786    81 TT--VVWDRE--------TGKPVYNAIVWQDRRTADICEELKAEGH 116
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
12-182 4.71e-09

nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466803 [Multi-domain]  Cd Length: 501  Bit Score: 58.73  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdAT-- 87
Cdd:cd07793     1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  88 CSLVVLDKE----FHplpvnhegdssrNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVM-----------------SVE 145
Cdd:cd07793    80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRsLLLKALRGGSKFLhfltrnkrflaasvlkfSTA 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039768924 146 MQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG 182
Cdd:cd07793   148 HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTG 187
PRK10331 PRK10331
L-fuculokinase; Provisional
17-288 1.36e-07

L-fuculokinase; Provisional


Pssm-ID: 182383 [Multi-domain]  Cd Length: 470  Bit Score: 53.88  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  17 DVGTGSVRAALVDQRGLLLAFAEQP----IKKWEPQFnhHEQSSEDIW---AACClvtKEVVQGIDAHRIRGL-----GF 84
Cdd:PRK10331    8 DCGATNVRAIAVDRQGKIVARASTPnasdIAAENSDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttfGV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  85 DATcslvvldkefhplPVNHEGDSSRNVIMWLDHRAVSQVHRI-NETKHRVLQYVGGVMSVEMQAP-KLLWLKENLREIc 162
Cdd:PRK10331   83 DGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQL- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 163 WDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGL-EDL---IDDNYSKIGNlvllpgaalg 236
Cdd:PRK10331  149 LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLsRRLfprLVEAGEQIGT---------- 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039768924 237 igLTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrGHGLtceGQPVTS 288
Cdd:PRK10331  218 --LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVLS 258
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
12-182 5.36e-07

nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466796 [Multi-domain]  Cd Length: 436  Bit Score: 51.84  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWEPQ--FNHHEQSSEDIWAAcclvTKEVVQGIDAH---RIRGLGFd 85
Cdd:cd07777     1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPREylsDVTGIGI- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  86 aTC---SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGV-MSVEMQAPKLLWLKENLREI 161
Cdd:cd07777    76 -TGqmhGIVLWDEDGNPV---------SPLITWQDQRCSEEFLGGLSTYGEELLPKSGMrLKPGYGLATLFWLLRNGPLP 145
                         170       180
                  ....*....|....*....|.
gi 1039768924 162 cwDKAGHFFDLPDFLSWKATG 182
Cdd:cd07777   146 --SKADRAGTIGDYIVARLTG 164
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
13-161 5.75e-07

nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466802 [Multi-domain]  Cd Length: 499  Bit Score: 52.14  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  13 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC--CL---VTKEVVQGIDAHRIRGLGFda 86
Cdd:cd07792     2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyeCIeeaVEKLKALGISPSDIKAIGI-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  87 TC---SLVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHR----INETKHRVLQYVGGVMSVEMQAPKLLWLKENLR 159
Cdd:cd07792    80 TNqreTTVVWDKS--------TGKPLYNAIVWLDTRTSDTVEElsakTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVP 151

                  ..
gi 1039768924 160 EI 161
Cdd:cd07792   152 EV 153
ASKHA_NBD_FGGY_NaCK-like cd07772
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ...
16-261 5.93e-04

nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466792 [Multi-domain]  Cd Length: 424  Bit Score: 42.25  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  16 IDVGTGSVRAALVDQRGLLLAFAEQPIK-KWEPQFNHHEqsSEDIWAACCLVTKEVVQGidaHRIRGLGFdaTC---SLV 91
Cdd:cd07772     5 FDIGKTNKKLLLFDENGEVLAERSTPNPeIEEDGYPCED--VEAIWEWLLDSLAELAKR---HRIDAINF--TThgaTFA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  92 VLDKEFHP-LPV---NHEGDSSrnvimwldhravsqvhrINEtkhrvlQY--------------VGGVMSVEMQapkLLW 153
Cdd:cd07772    78 LLDENGELaLPVydyEKPIPDE-----------------INE------AYyaergpfeetgsppLPGGLNLGKQ---LYW 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924 154 LKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledliddnys 222
Cdd:cd07772   132 LKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------ 198
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1039768924 223 kignlvLLPGAALGIgLTPEAARELGLPSGIAVAASLID 261
Cdd:cd07772   199 ------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHD 230
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
13-161 1.68e-03

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 41.11  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  13 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIdahRIRGLGFDATC--- 88
Cdd:PTZ00294    3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKL---REKGPSFKIKAigi 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039768924  89 -----SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINET--KHRVLQYVGG-VMSVEMQAPKLLWLKENLRE 160
Cdd:PTZ00294   80 tnqreTVVAWDK--------VTGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151

                  .
gi 1039768924 161 I 161
Cdd:PTZ00294  152 V 152
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
11-84 2.02e-03

Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];


Pssm-ID: 441543 [Multi-domain]  Cd Length: 306  Bit Score: 40.27  E-value: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039768924  11 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIkkwepqfnHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGF 84
Cdd:COG1940     5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPT--------PAGAGPEAVLEAIAELIEELLAeaGISRGRILGIGI 72
 
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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