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Conserved domains on  [gi|488984355|ref|WP_002895147|]
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MULTISPECIES: galactose-1-phosphate uridylyltransferase [Klebsiella]

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;
1-346 0e+00

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


:

Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 805.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   1 MSVFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFA 80
Cdd:PRK11720   1 MTQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  81 ALMTDTPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKSYPWVQVFENKGAAMGC 160
Cdd:PRK11720  81 ALMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 161 SNPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAH 240
Cdd:PRK11720 161 SNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 241 VQRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
Cdd:PRK11720 241 VLRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENDHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
                        330       340
                 ....*....|....*....|....*.
gi 488984355 321 ETQRDLTAEQAAERLRAVSDVHFRES 346
Cdd:PRK11720 321 ETQRDLTAEQAAERLRAVSDIHYRES 346
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-346 0e+00

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 805.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   1 MSVFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFA 80
Cdd:PRK11720   1 MTQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  81 ALMTDTPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKSYPWVQVFENKGAAMGC 160
Cdd:PRK11720  81 ALMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 161 SNPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAH 240
Cdd:PRK11720 161 SNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 241 VQRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
Cdd:PRK11720 241 VLRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENDHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
                        330       340
                 ....*....|....*....|....*.
gi 488984355 321 ETQRDLTAEQAAERLRAVSDVHFRES 346
Cdd:PRK11720 321 ETQRDLTAEQAAERLRAVSDIHYRES 346
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
1-347 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: 681.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355    1 MSVFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFA 80
Cdd:TIGR00209   1 MTQFNPVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLPAYDPDCYLCPGNKRVTGDLNPDYTGTYVFTNDFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   81 ALMTDTPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKSYPWVQVFENKGAAMGC 160
Cdd:TIGR00209  81 ALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  161 SNPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAH 240
Cdd:TIGR00209 161 SNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  241 VQRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
Cdd:TIGR00209 241 VLRITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPFNGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLG 320
                         330       340
                  ....*....|....*....|....*..
gi 488984355  321 ETQRDLTAEQAAERLRAVSDVHFRESG 347
Cdd:TIGR00209 321 ETQRDLTAEQAAERLRALSDIHYRERG 347
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
11-338 0e+00

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: 524.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  11 HRRYNPLTGQWILVSPHRAKRPWQGAQETPakQTLPAHDPDCFLCPGNTR-VTGDTNPNYTgTYVFTNDFAALMTDTPDA 89
Cdd:cd00608    1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEAP--KKLPEYDPDCPLCPGNERaDTGEQNPDYD-VRVFENDFPALKPDAPAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  90 PESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGK--SYPWVQVFENKGAAMGCSNPHPHG 167
Cdd:cd00608   78 EDSDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 168 QVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAHVQRITDL 247
Cdd:cd00608  158 QIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 248 TDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLA-ETQRDL 326
Cdd:cd00608  238 TDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPTGGKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFINDV 317
                        330
                 ....*....|..
gi 488984355 327 TAEQAAERLRAV 338
Cdd:cd00608  318 TPEQAAARLREV 329
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
5-341 0e+00

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 508.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   5 NPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQtlPAHDPDCFLCPGNTRVT-GDTNPNYTGTYVFTNDFAALM 83
Cdd:COG1085    1 PPPDMPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPEDP--PEYDEDCPLCPGNERATpPEIPPPGWDVRVFPNKFPALS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  84 TDTPDAPEsDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGK--SYPWVQVFENKGAAMGCS 161
Cdd:COG1085   79 PEAPDARE-GDGLYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGAdpRIRYVQIFENRGAEAGAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 162 NPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAHV 241
Cdd:COG1085  158 LPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 242 QRITDLTDAQRSDLALALKKLTSRYDNLFQCsFPYSMGWHGAPFNDEDHNHWQLHAHFYPPlLRSATVRKFMVGYEMLAE 321
Cdd:COG1085  238 SDFEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPVDGEERDHYHWHLEIYPR-LRSATVLKFLAGFELGAG 315
                        330       340
                 ....*....|....*....|.
gi 488984355 322 T-QRDLTAEQAAERLRAVSDV 341
Cdd:COG1085  316 AfINDVTPEQAAERLREVSEV 336
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
4-176 2.49e-96

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: 283.41  E-value: 2.49e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355    4 FNPVDH---PHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFA 80
Cdd:pfam01087   2 FEETDHiylSHRRYNPLTGEWVLVSPHRLKRPWAGQQEKISKDTLPEYDPMCYLCPGPSRANGDFNPDYKSPFVFTNDFY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   81 ALMTDTPDAPE---SDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKS--YPWVQVFENKG 155
Cdd:pfam01087  82 ALSKDNPYIKTdaiAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGASsyPKCVLCFENEG 161
                         170       180
                  ....*....|....*....|.
gi 488984355  156 AAMGCSNPHPHGQVWANSFLP 176
Cdd:pfam01087 162 YAMGCSNPHPHGQIWASSHLP 182
 
Name Accession Description Interval E-value
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
1-346 0e+00

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 805.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   1 MSVFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFA 80
Cdd:PRK11720   1 MTQFNPVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAKETLPAYDPDCFLCPGNTRVTGDVNPDYTGTYVFTNDFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  81 ALMTDTPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKSYPWVQVFENKGAAMGC 160
Cdd:PRK11720  81 ALMPDTPDAPESDDPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVFENKGAAMGC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 161 SNPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAH 240
Cdd:PRK11720 161 SNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLLPKAH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 241 VQRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
Cdd:PRK11720 241 VLRLTDLTDAQRDDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNGEENDHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
                        330       340
                 ....*....|....*....|....*.
gi 488984355 321 ETQRDLTAEQAAERLRAVSDVHFRES 346
Cdd:PRK11720 321 ETQRDLTAEQAAERLRAVSDIHYRES 346
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
1-347 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: 681.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355    1 MSVFNPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFA 80
Cdd:TIGR00209   1 MTQFNPVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQVLPAYDPDCYLCPGNKRVTGDLNPDYTGTYVFTNDFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   81 ALMTDTPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKSYPWVQVFENKGAAMGC 160
Cdd:TIGR00209  81 ALMSDTPDAPESHDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIFENKGAAMGC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  161 SNPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAH 240
Cdd:TIGR00209 161 SNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLPKAH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  241 VQRITDLTDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLA 320
Cdd:TIGR00209 241 VLRITDLTDAQRSDLALILKKLTSKYDNLFETSFPYSMGWHGAPFNGEENQHWQLHAHFYPPLLRSATVRKFMVGYEMLG 320
                         330       340
                  ....*....|....*....|....*..
gi 488984355  321 ETQRDLTAEQAAERLRAVSDVHFRESG 347
Cdd:TIGR00209 321 ETQRDLTAEQAAERLRALSDIHYRERG 347
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
11-338 0e+00

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: 524.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  11 HRRYNPLTGQWILVSPHRAKRPWQGAQETPakQTLPAHDPDCFLCPGNTR-VTGDTNPNYTgTYVFTNDFAALMTDTPDA 89
Cdd:cd00608    1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEAP--KKLPEYDPDCPLCPGNERaDTGEQNPDYD-VRVFENDFPALKPDAPAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  90 PESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGK--SYPWVQVFENKGAAMGCSNPHPHG 167
Cdd:cd00608   78 EDSDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKnpRIKYVQIFENKGAEMGASLPHPHG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 168 QVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAHVQRITDL 247
Cdd:cd00608  158 QIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 248 TDAQRSDLALALKKLTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLA-ETQRDL 326
Cdd:cd00608  238 TDEEREDLAEILKRLLARYDNLFNCSFPYSMGWHQAPTGGKELENWYYHWHFEIPPRRSATVLKFMAGFELGAgEFINDV 317
                        330
                 ....*....|..
gi 488984355 327 TAEQAAERLRAV 338
Cdd:cd00608  318 TPEQAAARLREV 329
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
5-341 0e+00

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 508.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   5 NPVDHPHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQtlPAHDPDCFLCPGNTRVT-GDTNPNYTGTYVFTNDFAALM 83
Cdd:COG1085    1 PPPDMPELRYDPLTGEWVLIAPHRAKRPWDGPVEKPEDP--PEYDEDCPLCPGNERATpPEIPPPGWDVRVFPNKFPALS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  84 TDTPDAPEsDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGK--SYPWVQVFENKGAAMGCS 161
Cdd:COG1085   79 PEAPDARE-GDGLYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGAdpRIRYVQIFENRGAEAGAS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 162 NPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAHV 241
Cdd:COG1085  158 LPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRHV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 242 QRITDLTDAQRSDLALALKKLTSRYDNLFQCsFPYSMGWHGAPFNDEDHNHWQLHAHFYPPlLRSATVRKFMVGYEMLAE 321
Cdd:COG1085  238 SDFEELTDEERDDLARILKRVLRRLDNLLGD-FPYNMGLHQAPVDGEERDHYHWHLEIYPR-LRSATVLKFLAGFELGAG 315
                        330       340
                 ....*....|....*....|.
gi 488984355 322 T-QRDLTAEQAAERLRAVSDV 341
Cdd:COG1085  316 AfINDVTPEQAAERLREVSEV 336
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
4-176 2.49e-96

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: 283.41  E-value: 2.49e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355    4 FNPVDH---PHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTLPAHDPDCFLCPGNTRVTGDTNPNYTGTYVFTNDFA 80
Cdd:pfam01087   2 FEETDHiylSHRRYNPLTGEWVLVSPHRLKRPWAGQQEKISKDTLPEYDPMCYLCPGPSRANGDFNPDYKSPFVFTNDFY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355   81 ALMTDTPDAPE---SDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLGKS--YPWVQVFENKG 155
Cdd:pfam01087  82 ALSKDNPYIKTdaiAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGASsyPKCVLCFENEG 161
                         170       180
                  ....*....|....*....|.
gi 488984355  156 AAMGCSNPHPHGQVWANSFLP 176
Cdd:pfam01087 162 YAMGCSNPHPHGQIWASSHLP 182
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
182-347 2.95e-94

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: 277.82  E-value: 2.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  182 EDRLQKEYYAAQGQPMLLDYVQRELADGSRTVVDTEHWLAVVPYWAAWPFETLLLPKAHVQRITDLTDAQRSDLALALKK 261
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  262 LTSRYDNLFQCSFPYSMGWHGAPFNDEDHNHWQLHAHFYPPLLRSATVRKFMVGYEMLAETQRDLTAEQAAERLRAVSDV 341
Cdd:pfam02744  81 LTRRYDNLFETSFPYSMGIHQAPLNAEELNHWQFHPHFYPPLLRSATVRKFMVGLEILGERQRDLTAEQAAERLRALSEV 160

                  ....*.
gi 488984355  342 HFRESG 347
Cdd:pfam02744 161 HYRWAL 166
PLN02643 PLN02643
ADP-glucose phosphorylase
10-295 1.77e-40

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 144.90  E-value: 1.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  10 PHRRYNPLTGQWILVSPHRAKRPWQGAQETPAKQTlPAHDPDCFLCPGNTRVTGD---------TNPNYTgTYVFTNDFA 80
Cdd:PLN02643   2 AELRKDPVTNRWVIFSPARGKRPTDFKSKSPQNPN-GNHSSGCPFCIGHEHECAPeifrvpddaSAPDWK-VRVIENLYP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  81 ALMTD---TPDAPESDDPLMRCQSARGTSRVICFSPDHSKTLPELSLEALEDVVKTWQEQTADLG--KSYPWVQVFENKG 155
Cdd:PLN02643  80 ALSRDlepPCTEGQGEDYGGRRLPGFGFHDVVIETPVHSVQLSDLPARHIGEVLKAYKKRINQLQsdSRFKYVQVFKNHG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 156 AAMGCSNPHPHGQVWANSFLPNEAEREDRLQKEYYAAQGQPMLLDYVQRELadgsrtVVD-TEHWLAVVPYWAAWPFETL 234
Cdd:PLN02643 160 ASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYFEKTGKCSLCEVVKKDL------LIDeSSHFVSIAPFAATFPFEIW 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488984355 235 LLPKAHVQRITDLTDAQRSDLALALKKLTSRYDNLFQCSfPYSMGWHGAPFNDED----HNHWQL 295
Cdd:PLN02643 234 IIPRDHSSNFHEIDDDKAVDLGGLLKLMLQKISKQLNDP-PYNYMIQTSPLGVEEsnlpYTHWFL 297
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
66-171 1.43e-23

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: 92.92  E-value: 1.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355  66 NPNYTGTYVFTNDFAAlmtdtpdapesddplmrcqsaRGTSRVICFsPDHSKTLPELSLEALEDVVKTWQEQTADL--GK 143
Cdd:cd00468    1 VPDDEHSFAFVNLKPA---------------------APGHVLVCP-KRHVETLPDLDEALLADLVITAQRVAAELekHG 58
                         90       100
                 ....*....|....*....|....*...
gi 488984355 144 SYPWVQVFENKGAAMGCSNPHPHGQVWA 171
Cdd:cd00468   59 NVPSLTVFVNDGAAAGQSVPHVHLHVLP 86
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
210-337 1.03e-04

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: 41.47  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488984355 210 SRTVVDTEHWLAVV---PYWAAWpfeTLLLPKAHVQRITDLTDAQRSDLALALKKLTSRYDNLFQCS-FPYSMGWHGAPF 285
Cdd:COG0537   15 ALIVYEDEHVLAFLdinPYAPGH---TLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDgFNLGINNGEAAG 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488984355 286 NDEDHnhwqLHAHFYPpllRSATVRKFMVGYEMLAETQRdltAEQAAERLRA 337
Cdd:COG0537   92 QTVPH----LHVHVIP---RYEGDDNFMPVIGTKVDPEE---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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