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Conserved domains on  [gi|757597327|ref|WP_042844984|]
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MULTISPECIES: UDP-glucose--hexose-1-phosphate uridylyltransferase [Providencia]

Protein Classification

galactose-1-phosphate uridylyltransferase( domain architecture ID 11485466)

galactose-1-phosphate uridylyltransferase catalyzes the reversible transfer of the uridine 5'-monophosphoryl moiety of UDP-glucose to the phosphate group of galactose 1-phosphate to form UDP-galactose in the third step of the Leloir pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
4-350 0e+00

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


:

Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 705.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   4 MPFNPSDCPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSITDLPEYDKNCFLCPTNTRVSGEVNPNYQGTYVFQNDHGA 83
Cdd:PRK11720   2 TQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  84 LLEQACVQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSKQFTWVQVFENKGEIMGCS 163
Cdd:PRK11720  82 LMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 164 QPHPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPI 243
Cdd:PRK11720 162 NPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 244 RRMDEMNETVRTDLSLALKKLTCRYDNLFQCSFPYSMGWHFAPYFkpHKDIEHWQLHALFYPPLLRSATVKKFMVGYEML 323
Cdd:PRK11720 242 LRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFN--GEENDHWQLHAHFYPPLLRSATVRKFMVGYEML 319
                        330       340
                 ....*....|....*....|....*..
gi 757597327 324 AETQRDLTPEQAAQRLREVSEIHYKQR 350
Cdd:PRK11720 320 AETQRDLTAEQAAERLRAVSDIHYRES 346
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
4-350 0e+00

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 705.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   4 MPFNPSDCPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSITDLPEYDKNCFLCPTNTRVSGEVNPNYQGTYVFQNDHGA 83
Cdd:PRK11720   2 TQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  84 LLEQACVQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSKQFTWVQVFENKGEIMGCS 163
Cdd:PRK11720  82 LMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 164 QPHPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPI 243
Cdd:PRK11720 162 NPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 244 RRMDEMNETVRTDLSLALKKLTCRYDNLFQCSFPYSMGWHFAPYFkpHKDIEHWQLHALFYPPLLRSATVKKFMVGYEML 323
Cdd:PRK11720 242 LRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFN--GEENDHWQLHAHFYPPLLRSATVRKFMVGYEML 319
                        330       340
                 ....*....|....*....|....*..
gi 757597327 324 AETQRDLTPEQAAQRLREVSEIHYKQR 350
Cdd:PRK11720 320 AETQRDLTAEQAAERLRAVSDIHYRES 346
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
6-350 0e+00

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: 534.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327    6 FNPSDCPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSITDLPEYDKNCFLCPTNTRVSGEVNPNYQGTYVFQNDHGALL 85
Cdd:TIGR00209   4 FNPVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLPAYDPDCYLCPGNKRVTGDLNPDYTGTYVFTNDFAALM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   86 EQACVQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSKQFTWVQVFENKGEIMGCSQP 165
Cdd:TIGR00209  84 SDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGCSNP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  166 HPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPIRR 245
Cdd:TIGR00209 164 HPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHVLR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  246 MDEMNETVRTDLSLALKKLTCRYDNLFQCSFPYSMGWHFAPYfkPHKDIEHWQLHALFYPPLLRSATVKKFMVGYEMLAE 325
Cdd:TIGR00209 244 ITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPF--NGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLGE 321
                         330       340
                  ....*....|....*....|....*
gi 757597327  326 TQRDLTPEQAAQRLREVSEIHYKQR 350
Cdd:TIGR00209 322 TQRDLTAEQAAERLRALSDIHYRER 346
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
7-345 5.64e-167

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 468.54  E-value: 5.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   7 NPSDCPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSitDLPEYDKNCFLCPTNTRV-SGEVNPNYQGTYVFQNDHGALL 85
Cdd:COG1085    1 PPPDMPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPE--DPPEYDEDCPLCPGNERAtPPEIPPPGWDVRVFPNKFPALS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  86 EQACVQPENQSaLFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSKQ--FTWVQVFENKGEIMGCS 163
Cdd:COG1085   79 PEAPDAREGDG-LYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 164 QPHPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPI 243
Cdd:COG1085  158 LPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 244 RRMDEMNETVRTDLSLALKKLTCRYDNLFQCsFPYSMGWHFAPYfkPHKDIEHWQLHALFYPPlLRSATVKKFMVGYEML 323
Cdd:COG1085  238 SDFEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPV--DGEERDHYHWHLEIYPR-LRSATVLKFLAGFELG 313
                        330       340
                 ....*....|....*....|...
gi 757597327 324 AET-QRDLTPEQAAQRLREVSEI 345
Cdd:COG1085  314 AGAfINDVTPEQAAERLREVSEV 336
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
13-342 1.67e-162

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: 457.15  E-value: 1.67e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  13 HRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSitDLPEYDKNCFLCPTNTR-VSGEVNPNYQgTYVFQNDHGALLEQACVQ 91
Cdd:cd00608    1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEAPK--KLPEYDPDCPLCPGNERaDTGEQNPDYD-VRVFENDFPALKPDAPAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  92 PENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSK--QFTWVQVFENKGEIMGCSQPHPHG 169
Cdd:cd00608   78 EDSDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 170 QIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPIRRMDEM 249
Cdd:cd00608  158 QIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 250 NETVRTDLSLALKKLTCRYDNLFQCSFPYSMGWHFAPYfkPHKDIEHWQLHALFYPPLLRSATVKKFMVGYEMLA-ETQR 328
Cdd:cd00608  238 TDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPT--GGKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFIN 315
                        330
                 ....*....|....
gi 757597327 329 DLTPEQAAQRLREV 342
Cdd:cd00608  316 DVTPEQAAARLREV 329
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
5-178 1.47e-86

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: 258.76  E-value: 1.47e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327    5 PFNPSD---CPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSITDLPEYDKNCFLCPTNTRVSGEVNPNYQGTYVFQNDH 81
Cdd:pfam01087   1 LFEETDhiyLSHRRYNPLTGEWVLVSPHRLKRPWAGQQEKISKDTLPEYDPMCYLCPGPSRANGDFNPDYKSPFVFTNDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   82 GALLEQAC---VQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTEL--SKQFTWVQVFENK 156
Cdd:pfam01087  81 YALSKDNPyikTDAIAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELgaSSYPKCVLCFENE 160
                         170       180
                  ....*....|....*....|..
gi 757597327  157 GEIMGCSQPHPHGQIWASDFLP 178
Cdd:pfam01087 161 GYAMGCSNPHPHGQIWASSHLP 182
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
4-350 0e+00

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 705.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   4 MPFNPSDCPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSITDLPEYDKNCFLCPTNTRVSGEVNPNYQGTYVFQNDHGA 83
Cdd:PRK11720   2 TQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  84 LLEQACVQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSKQFTWVQVFENKGEIMGCS 163
Cdd:PRK11720  82 LMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGCS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 164 QPHPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPI 243
Cdd:PRK11720 162 NPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAHV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 244 RRMDEMNETVRTDLSLALKKLTCRYDNLFQCSFPYSMGWHFAPYFkpHKDIEHWQLHALFYPPLLRSATVKKFMVGYEML 323
Cdd:PRK11720 242 LRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFN--GEENDHWQLHAHFYPPLLRSATVRKFMVGYEML 319
                        330       340
                 ....*....|....*....|....*..
gi 757597327 324 AETQRDLTPEQAAQRLREVSEIHYKQR 350
Cdd:PRK11720 320 AETQRDLTAEQAAERLRAVSDIHYRES 346
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
6-350 0e+00

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: 534.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327    6 FNPSDCPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSITDLPEYDKNCFLCPTNTRVSGEVNPNYQGTYVFQNDHGALL 85
Cdd:TIGR00209   4 FNPVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLPAYDPDCYLCPGNKRVTGDLNPDYTGTYVFTNDFAALM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   86 EQACVQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSKQFTWVQVFENKGEIMGCSQP 165
Cdd:TIGR00209  84 SDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGCSNP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  166 HPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPIRR 245
Cdd:TIGR00209 164 HPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAHVLR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  246 MDEMNETVRTDLSLALKKLTCRYDNLFQCSFPYSMGWHFAPYfkPHKDIEHWQLHALFYPPLLRSATVKKFMVGYEMLAE 325
Cdd:TIGR00209 244 ITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPF--NGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLGE 321
                         330       340
                  ....*....|....*....|....*
gi 757597327  326 TQRDLTPEQAAQRLREVSEIHYKQR 350
Cdd:TIGR00209 322 TQRDLTAEQAAERLRALSDIHYRER 346
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
7-345 5.64e-167

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 468.54  E-value: 5.64e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   7 NPSDCPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSitDLPEYDKNCFLCPTNTRV-SGEVNPNYQGTYVFQNDHGALL 85
Cdd:COG1085    1 PPPDMPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPE--DPPEYDEDCPLCPGNERAtPPEIPPPGWDVRVFPNKFPALS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  86 EQACVQPENQSaLFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSKQ--FTWVQVFENKGEIMGCS 163
Cdd:COG1085   79 PEAPDAREGDG-LYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADprIRYVQIFENRGAEAGAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 164 QPHPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPI 243
Cdd:COG1085  158 LPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 244 RRMDEMNETVRTDLSLALKKLTCRYDNLFQCsFPYSMGWHFAPYfkPHKDIEHWQLHALFYPPlLRSATVKKFMVGYEML 323
Cdd:COG1085  238 SDFEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPV--DGEERDHYHWHLEIYPR-LRSATVLKFLAGFELG 313
                        330       340
                 ....*....|....*....|...
gi 757597327 324 AET-QRDLTPEQAAQRLREVSEI 345
Cdd:COG1085  314 AGAfINDVTPEQAAERLREVSEV 336
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
13-342 1.67e-162

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: 457.15  E-value: 1.67e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  13 HRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSitDLPEYDKNCFLCPTNTR-VSGEVNPNYQgTYVFQNDHGALLEQACVQ 91
Cdd:cd00608    1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEAPK--KLPEYDPDCPLCPGNERaDTGEQNPDYD-VRVFENDFPALKPDAPAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  92 PENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELSK--QFTWVQVFENKGEIMGCSQPHPHG 169
Cdd:cd00608   78 EDSDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 170 QIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPIRRMDEM 249
Cdd:cd00608  158 QIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 250 NETVRTDLSLALKKLTCRYDNLFQCSFPYSMGWHFAPYfkPHKDIEHWQLHALFYPPLLRSATVKKFMVGYEMLA-ETQR 328
Cdd:cd00608  238 TDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPT--GGKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFIN 315
                        330
                 ....*....|....
gi 757597327 329 DLTPEQAAQRLREV 342
Cdd:cd00608  316 DVTPEQAAARLREV 329
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
5-178 1.47e-86

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: 258.76  E-value: 1.47e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327    5 PFNPSD---CPHRRYNPLTGQWVLVSPHRAKRPWSGQDEKPSITDLPEYDKNCFLCPTNTRVSGEVNPNYQGTYVFQNDH 81
Cdd:pfam01087   1 LFEETDhiyLSHRRYNPLTGEWVLVSPHRLKRPWAGQQEKISKDTLPEYDPMCYLCPGPSRANGDFNPDYKSPFVFTNDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327   82 GALLEQAC---VQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTEL--SKQFTWVQVFENK 156
Cdd:pfam01087  81 YALSKDNPyikTDAIAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELgaSSYPKCVLCFENE 160
                         170       180
                  ....*....|....*....|..
gi 757597327  157 GEIMGCSQPHPHGQIWASDFLP 178
Cdd:pfam01087 161 GYAMGCSNPHPHGQIWASSHLP 182
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
191-350 1.51e-74

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: 227.75  E-value: 1.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  191 YYQRHGSNLLMDYVNAEQKSGARTVVETEYWIAVVPYWAAWPFETMLLPKQPIRRMDEMNETVRTDLSLALKKLTCRYDN 270
Cdd:pfam02744   8 YFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKPLTRRYDN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  271 LFQCSFPYSMGWHFAPYfkPHKDIEHWQLHALFYPPLLRSATVKKFMVGYEMLAETQRDLTPEQAAQRLREVSEIHYKQR 350
Cdd:pfam02744  88 LFETSFPYSMGIHQAPL--NAEELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRALSEVHYRWA 165
PLN02643 PLN02643
ADP-glucose phosphorylase
12-343 5.44e-36

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 133.35  E-value: 5.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  12 PHRRYNPLTGQWVLVSPHRAKRPwSGQDEKPSITDLPEYDKNCFLCPTNT--------RVSGEVN-PNYQgTYVFQNDHG 82
Cdd:PLN02643   2 AELRKDPVTNRWVIFSPARGKRP-TDFKSKSPQNPNGNHSSGCPFCIGHEhecapeifRVPDDASaPDWK-VRVIENLYP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  83 AL---LEQACVQPENQSALFQTQSVRGVSRVICFSPDHSKTLPELSLPEIEKVVETWQQQVTELS--KQFTWVQVFENKG 157
Cdd:PLN02643  80 ALsrdLEPPCTEGQGEDYGGRRLPGFGFHDVVIETPVHSVQLSDLPARHIGEVLKAYKKRINQLQsdSRFKYVQVFKNHG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 158 EIMGCSQPHPHGQIWASDFLPNEIERKDHFLAQYYQRHGSNLLMDYVNAEqksgarTVV-ETEYWIAVVPYWAAWPFETM 236
Cdd:PLN02643 160 ASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYFEKTGKCSLCEVVKKD------LLIdESSHFVSIAPFAATFPFEIW 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327 237 LLPKQPIRRMDEMNETVRTDLSLALKKLTCRYDNLFQCSfPYSMGWHFAPYFKPHKDIE--HWQLHALfyPPLlrsATVK 314
Cdd:PLN02643 234 IIPRDHSSNFHEIDDDKAVDLGGLLKLMLQKISKQLNDP-PYNYMIQTSPLGVEESNLPytHWFLQIV--PQL---SGVG 307
                        330       340
                 ....*....|....*....|....*....
gi 757597327 315 KFMVGYEMLAETQRdltPEQAAQRLREVS 343
Cdd:PLN02643 308 GFELGTGCYINPVF---PEDAAKVLREVN 333
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
68-173 1.16e-15

HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups.


Pssm-ID: 238263 [Multi-domain]  Cd Length: 86  Bit Score: 71.35  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757597327  68 NPNYQGTYVFQNDHGAlleqacvqpenqsalfqtqsvRGVSRVICFsPDHSKTLPELSLPEIEKVVETWQQQVTELSKQF 147
Cdd:cd00468    1 VPDDEHSFAFVNLKPA---------------------APGHVLVCP-KRHVETLPDLDEALLADLVITAQRVAAELEKHG 58
                         90       100
                 ....*....|....*....|....*...
gi 757597327 148 --TWVQVFENKGEIMGCSQPHPHGQIWA 173
Cdd:cd00468   59 nvPSLTVFVNDGAAAGQSVPHVHLHVLP 86
 
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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