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Conserved domains on  [gi|700274118|ref|NP_001289440|]
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galactose-1-phosphate uridylyltransferase isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11720 super family cl29677
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-190 2.00e-133

UDP-glucose--hexose-1-phosphate uridylyltransferase;


The actual alignment was detected with superfamily member PRK11720:

Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 377.71  E-value: 2.00e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   1 MMGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLL 80
Cdd:PRK11720 157 AMGCSNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  81 PRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFM 160
Cdd:PRK11720 237 PKAHVLRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFN---GEENDHWQLHAHFYPPLLRSATVRKFM 313
                        170       180       190
                 ....*....|....*....|....*....|
gi 700274118 161 VGYEMLAQAQRDLTPEQAAERLRALPEVHY 190
Cdd:PRK11720 314 VGYEMLAETQRDLTAEQAAERLRAVSDIHY 343
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-190 2.00e-133

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 377.71  E-value: 2.00e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   1 MMGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLL 80
Cdd:PRK11720 157 AMGCSNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  81 PRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFM 160
Cdd:PRK11720 237 PKAHVLRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFN---GEENDHWQLHAHFYPPLLRSATVRKFM 313
                        170       180       190
                 ....*....|....*....|....*....|
gi 700274118 161 VGYEMLAQAQRDLTPEQAAERLRALPEVHY 190
Cdd:PRK11720 314 VGYEMLAETQRDLTAEQAAERLRAVSDIHY 343
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
2-190 9.76e-101

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 294.95  E-value: 9.76e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118    2 MGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLP 81
Cdd:TIGR00209 158 MGCSNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLP 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   82 RRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTglkTGATCDHWQLHAHYYPPLLRSATVRKFMV 161
Cdd:TIGR00209 238 KAHVLRITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPF---NGEENQHWQLHAHFYPPLLRSATVRKFMV 314
                         170       180
                  ....*....|....*....|....*....
gi 700274118  162 GYEMLAQAQRDLTPEQAAERLRALPEVHY 190
Cdd:TIGR00209 315 GYEMLGETQRDLTAEQAAERLRALSDIHY 343
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
1-185 2.04e-99

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 290.74  E-value: 2.04e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   1 MMGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLL 80
Cdd:cd00608  147 EMGASLPHPHGQIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHIL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  81 PRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFM 160
Cdd:cd00608  227 PKRHVSRFTDLTDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFM 303
                        170       180
                 ....*....|....*....|....*.
gi 700274118 161 VGYEMLA-QAQRDLTPEQAAERLRAL 185
Cdd:cd00608  304 AGFELGAgEFINDVTPEQAAARLREV 329
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
1-188 7.35e-90

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 266.70  E-value: 7.35e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   1 MMGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLL 80
Cdd:COG1085  153 EAGASLPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWIL 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  81 PRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETsFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPlLRSATVRKFM 160
Cdd:COG1085  233 PKRHVSDFEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPVD---GEERDHYHWHLEIYPR-LRSATVLKFL 307
                        170       180
                 ....*....|....*....|....*....
gi 700274118 161 VGYEMLAQA-QRDLTPEQAAERLRALPEV 188
Cdd:COG1085  308 AGFELGAGAfINDVTPEQAAERLREVSEV 336
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
26-194 2.54e-87

Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 397044 [Multi-domain]  Cd Length: 166  Bit Score: 254.33  E-value: 2.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   26 EERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKK 105
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  106 LLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRAL 185
Cdd:pfam02744  81 LTRRYDNLFETSFPYSMGIHQAPLN---AEELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRAL 157

                  ....*....
gi 700274118  186 PEVHYCLAQ 194
Cdd:pfam02744 158 SEVHYRWAL 166
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-190 2.00e-133

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 377.71  E-value: 2.00e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   1 MMGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLL 80
Cdd:PRK11720 157 AMGCSNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLL 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  81 PRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFM 160
Cdd:PRK11720 237 PKAHVLRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFN---GEENDHWQLHAHFYPPLLRSATVRKFM 313
                        170       180       190
                 ....*....|....*....|....*....|
gi 700274118 161 VGYEMLAQAQRDLTPEQAAERLRALPEVHY 190
Cdd:PRK11720 314 VGYEMLAETQRDLTAEQAAERLRAVSDIHY 343
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
2-190 9.76e-101

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 294.95  E-value: 9.76e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118    2 MGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLP 81
Cdd:TIGR00209 158 MGCSNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLP 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   82 RRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTglkTGATCDHWQLHAHYYPPLLRSATVRKFMV 161
Cdd:TIGR00209 238 KAHVLRITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPF---NGEENQHWQLHAHFYPPLLRSATVRKFMV 314
                         170       180
                  ....*....|....*....|....*....
gi 700274118  162 GYEMLAQAQRDLTPEQAAERLRALPEVHY 190
Cdd:TIGR00209 315 GYEMLGETQRDLTAEQAAERLRALSDIHY 343
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
1-185 2.04e-99

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 290.74  E-value: 2.04e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   1 MMGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLL 80
Cdd:cd00608  147 EMGASLPHPHGQIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHIL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  81 PRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFM 160
Cdd:cd00608  227 PKRHVSRFTDLTDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPTG---GKELENWYYHWHFEIPPRRSATVLKFM 303
                        170       180
                 ....*....|....*....|....*.
gi 700274118 161 VGYEMLA-QAQRDLTPEQAAERLRAL 185
Cdd:cd00608  304 AGFELGAgEFINDVTPEQAAARLREV 329
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
1-188 7.35e-90

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 266.70  E-value: 7.35e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   1 MMGCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLL 80
Cdd:COG1085  153 EAGASLPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWIL 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  81 PRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETsFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPlLRSATVRKFM 160
Cdd:COG1085  233 PKRHVSDFEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPVD---GEERDHYHWHLEIYPR-LRSATVLKFL 307
                        170       180
                 ....*....|....*....|....*....
gi 700274118 161 VGYEMLAQA-QRDLTPEQAAERLRALPEV 188
Cdd:COG1085  308 AGFELGAGAfINDVTPEQAAERLREVSEV 336
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
26-194 2.54e-87

Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 397044 [Multi-domain]  Cd Length: 166  Bit Score: 254.33  E-value: 2.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   26 EERSQQTYHSQHGKPLLLEYGHQELLRKERLVLTSEHWIVLVPFWAVWPFQTLLLPRRHVRRLPELNPAERDDLASIMKK 105
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  106 LLTKYDNLFETSFPYSMGWHGAPTGlktGATCDHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRAL 185
Cdd:pfam02744  81 LTRRYDNLFETSFPYSMGIHQAPLN---AEELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRAL 157

                  ....*....
gi 700274118  186 PEVHYCLAQ 194
Cdd:pfam02744 158 SEVHYRWAL 166
PLN02643 PLN02643
ADP-glucose phosphorylase
3-142 4.26e-15

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 72.10  E-value: 4.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118   3 GCSNPHPHCQVWASSFLPDIAQREERSQQTYHSQHGKPLLLEYGHQELLRKErlvltSEHWIVLVPFWAVWPFQTLLLPR 82
Cdd:PLN02643 163 GASMSHSHSQIIALPVVPPSVSARLDGSKEYFEKTGKCSLCEVVKKDLLIDE-----SSHFVSIAPFAATFPFEIWIIPR 237
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 700274118  83 RHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSfPYSMGWHGAPTGLKTGATC-DHWQL 142
Cdd:PLN02643 238 DHSSNFHEIDDDKAVDLGGLLKLMLQKISKQLNDP-PYNYMIQTSPLGVEESNLPyTHWFL 297
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
1-20 3.43e-09

Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 426039 [Multi-domain]  Cd Length: 182  Bit Score: 53.83  E-value: 3.43e-09
                          10        20
                  ....*....|....*....|
gi 700274118    1 MMGCSNPHPHCQVWASSFLP 20
Cdd:pfam01087 163 AMGCSNPHPHGQIWASSHLP 182
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
77-184 2.53e-03

Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 440303 [Multi-domain]  Cd Length: 133  Bit Score: 36.47  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700274118  77 TLLLPRRHVRRLPELNPAERDDLASIMKKLLTKYDNLFETSfPYSMGWHgapTGLKTGATCDHwqLHAHYYPpllRSATV 156
Cdd:COG0537   38 TLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPD-GFNLGIN---NGEAAGQTVPH--LHVHVIP---RYEGD 108
                         90       100
                 ....*....|....*....|....*...
gi 700274118 157 RKFMVGYEMLAQAQRdltPEQAAERLRA 184
Cdd:COG0537  109 DNFMPVIGTKVDPEE---LEETARKLRA 133
 
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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