NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|494112963|ref|WP_007053742|]
View 

MULTISPECIES: galactose-1-phosphate uridylyltransferase [Bifidobacterium]

Protein Classification

galactose-1-phosphate uridylyltransferase( domain architecture ID 10089510)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
75-409 2.53e-144

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: 413.62  E-value: 2.53e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  75 QMRRDPLTGDWIPMATARMNRPITAGPGA------TAKGNPLAarkPGDPYQDGEVPDTDYNVVVFENRFPSMVRVPGVS 148
Cdd:cd00608    1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEApkklpeYDPDCPLC---PGNERADTGEQNPDYDVRVFENDFPALKPDAPAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 149 EDvtyvDGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFPFENHGQEIGVSLA 228
Cdd:cd00608   78 ED----SDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKNPRIKYVQIFENKGAEMGASLP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 229 HPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAPVRDVLT 308
Cdd:cd00608  154 HPHGQIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 309 LDQLNDEERWDLASMYSHLLKRGNAFFDKgdgkgmDLPYIAAWHQAPIHDARRENYRLNLQFFSF-RRAANKIKYLAGSE 387
Cdd:cd00608  234 FTDLTDEEREDLAEILKRLLARYDNLFNC------SFPYSMGWHQAPTGGKELENWYYHWHFEIPpRRSATVLKFMAGFE 307
                        330       340
                 ....*....|....*....|..
gi 494112963 388 SGMAAWISDTTPELIAKRFHEL 409
Cdd:cd00608  308 LGAGEFINDVTPEQAAARLREV 329
 
Name Accession Description Interval E-value
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
75-409 2.53e-144

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: 413.62  E-value: 2.53e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  75 QMRRDPLTGDWIPMATARMNRPITAGPGA------TAKGNPLAarkPGDPYQDGEVPDTDYNVVVFENRFPSMVRVPGVS 148
Cdd:cd00608    1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEApkklpeYDPDCPLC---PGNERADTGEQNPDYDVRVFENDFPALKPDAPAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 149 EDvtyvDGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFPFENHGQEIGVSLA 228
Cdd:cd00608   78 ED----SDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKNPRIKYVQIFENKGAEMGASLP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 229 HPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAPVRDVLT 308
Cdd:cd00608  154 HPHGQIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 309 LDQLNDEERWDLASMYSHLLKRGNAFFDKgdgkgmDLPYIAAWHQAPIHDARRENYRLNLQFFSF-RRAANKIKYLAGSE 387
Cdd:cd00608  234 FTDLTDEEREDLAEILKRLLARYDNLFNC------SFPYSMGWHQAPTGGKELENWYYHWHFEIPpRRSATVLKFMAGFE 307
                        330       340
                 ....*....|....*....|..
gi 494112963 388 SGMAAWISDTTPELIAKRFHEL 409
Cdd:cd00608  308 LGAGEFINDVTPEQAAARLREV 329
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
72-412 1.86e-140

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 404.21  E-value: 1.86e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  72 AAPQMRRDPLTGDWIPMATARMNRPI------TAGPGATAKGNPLAARKPGDPYqdGEVPDTDYNVVVFENRFPSMVRVP 145
Cdd:COG1085    4 DMPELRYDPLTGEWVLIAPHRAKRPWdgpvekPEDPPEYDEDCPLCPGNERATP--PEIPPPGWDVRVFPNKFPALSPEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 146 GVSEDvtyvdGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFPFENHGQEIGV 225
Cdd:COG1085   82 PDARE-----GDGLYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADPRIRYVQIFENRGAEAGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 226 SLAHPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAPVRD 305
Cdd:COG1085  157 SLPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRH 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 306 VLTLDQLNDEERWDLASMYSHLLKRGNAFFDkgdgkgmDLPYIAAWHQAPIHDARRENYRLNLQFFSFRRAANKIKYLAG 385
Cdd:COG1085  237 VSDFEELTDEERDDLARILKRVLRRLDNLLG-------DFPYNMGLHQAPVDGEERDHYHWHLEIYPRLRSATVLKFLAG 309
                        330       340
                 ....*....|....*....|....*..
gi 494112963 386 SESGMAAWISDTTPELIAKRFHELGSI 412
Cdd:COG1085  310 FELGAGAFINDVTPEQAAERLREVSEV 336
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
70-412 2.73e-53

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 180.88  E-value: 2.73e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  70 PYAAPQMRRDPLTGDWIPMATARMNRPITAGPGATAKgNPLAARK------PGDPYQDGEVpDTDY-NVVVFENRFPS-M 141
Cdd:PRK11720   6 PVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAK-ETLPAYDpdcflcPGNTRVTGDV-NPDYtGTYVFTNDFAAlM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 142 VRVPGVSEDVtyvdgNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFpfENHGQ 221
Cdd:PRK11720  84 PDTPDAPESD-----DPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVF--ENKGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 222 EIGVSLAHPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVA 301
Cdd:PRK11720 157 AMGCSNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 302 PVRDVLTLDQLNDEERWDLASMYSHLLKRGNAFFDkgdgkgMDLPYIAAWHQAPIHDARRENYRLNLQFF-SFRRAANKI 380
Cdd:PRK11720 237 PKAHVLRLTDLTDAQRDDLALALKKLTSRYDNLFQ------CSFPYSMGWHGAPFNGEENDHWQLHAHFYpPLLRSATVR 310
                        330       340       350
                 ....*....|....*....|....*....|..
gi 494112963 381 KYLAGSESgMAAWISDTTPELIAKRFHELGSI 412
Cdd:PRK11720 311 KFMVGYEM-LAETQRDLTAEQAAERLRAVSDI 341
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
70-412 1.92e-47

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: 165.52  E-value: 1.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963   70 PYAAPQMRRDPLTGDWIPMATARMNRPITAGPGATAKG-----NPLAARKPGDPYQDGEVpDTDY-NVVVFENRFPS-MV 142
Cdd:TIGR00209   6 PVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQvlpayDPDCYLCPGNKRVTGDL-NPDYtGTYVFTNDFAAlMS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  143 RVPGVSEDvtyvdGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFpfENHGQE 222
Cdd:TIGR00209  85 DTPDAPES-----HDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIF--ENKGAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  223 IGVSLAHPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAP 302
Cdd:TIGR00209 158 MGCSNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  303 VRDVLTLDQLNDEERWDLASMYSHLLKRGNAFFDkgdgkgMDLPYIAAWHQAPIHDARRENYRLNLQFF-SFRRAANKIK 381
Cdd:TIGR00209 238 KAHVLRITDLTDAQRSDLALILKKLTSKYDNLFE------TSFPYSMGWHGAPFNGEENQHWQLHAHFYpPLLRSATVRK 311
                         330       340       350
                  ....*....|....*....|....*....|.
gi 494112963  382 YLAGSESgMAAWISDTTPELIAKRFHELGSI 412
Cdd:TIGR00209 312 FMVGYEM-LGETQRDLTAEQAAERLRALSDI 341
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
73-240 1.24e-34

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: 126.64  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963   73 APQMRRDPLTGDWIPMATARMNRPItAGPGATAKGNPLAARKPGD-----PYQDGEVPDTDY-NVVVFENRFPSmvrvpg 146
Cdd:pfam01087  10 LSHRRYNPLTGEWVLVSPHRLKRPW-AGQQEKISKDTLPEYDPMCylcpgPSRANGDFNPDYkSPFVFTNDFYA------ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  147 VSEDVTYV-----DGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFPFENHGQ 221
Cdd:pfam01087  83 LSKDNPYIktdaiAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGASSYPKCVLCFENEGY 162
                         170
                  ....*....|....*....
gi 494112963  222 EIGVSLAHPHGQVYCYPFI 240
Cdd:pfam01087 163 AMGCSNPHPHGQIWASSHL 181
 
Name Accession Description Interval E-value
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
75-409 2.53e-144

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: 413.62  E-value: 2.53e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  75 QMRRDPLTGDWIPMATARMNRPITAGPGA------TAKGNPLAarkPGDPYQDGEVPDTDYNVVVFENRFPSMVRVPGVS 148
Cdd:cd00608    1 HRRYNPLTGEWVLVSPHRAKRPWQGQQEApkklpeYDPDCPLC---PGNERADTGEQNPDYDVRVFENDFPALKPDAPAP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 149 EDvtyvDGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFPFENHGQEIGVSLA 228
Cdd:cd00608   78 ED----SDDGLFRTAPARGRCEVICFSPDHNLTLAEMSVAEIREVVEAWAERTRELGKNPRIKYVQIFENKGAEMGASLP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 229 HPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAPVRDVLT 308
Cdd:cd00608  154 HPHGQIWALPFLPPEVARELRNQKAYYEKHGRCLLCDYLKLELESKERIVVENEHFVAVVPFWARWPFEVHILPKRHVSR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 309 LDQLNDEERWDLASMYSHLLKRGNAFFDKgdgkgmDLPYIAAWHQAPIHDARRENYRLNLQFFSF-RRAANKIKYLAGSE 387
Cdd:cd00608  234 FTDLTDEEREDLAEILKRLLARYDNLFNC------SFPYSMGWHQAPTGGKELENWYYHWHFEIPpRRSATVLKFMAGFE 307
                        330       340
                 ....*....|....*....|..
gi 494112963 388 SGMAAWISDTTPELIAKRFHEL 409
Cdd:cd00608  308 LGAGEFINDVTPEQAAARLREV 329
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
72-412 1.86e-140

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 404.21  E-value: 1.86e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  72 AAPQMRRDPLTGDWIPMATARMNRPI------TAGPGATAKGNPLAARKPGDPYqdGEVPDTDYNVVVFENRFPSMVRVP 145
Cdd:COG1085    4 DMPELRYDPLTGEWVLIAPHRAKRPWdgpvekPEDPPEYDEDCPLCPGNERATP--PEIPPPGWDVRVFPNKFPALSPEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 146 GVSEDvtyvdGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFPFENHGQEIGV 225
Cdd:COG1085   82 PDARE-----GDGLYDAMPGRGRHEVICFSPDHDLSLAELSVERIRDVLEAWRDRTAELGADPRIRYVQIFENRGAEAGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 226 SLAHPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAPVRD 305
Cdd:COG1085  157 SLPHPHGQIIAYPFVPPRIARELRGARAYYEEHGRCLLCDILAQELAAGERVVAENEHFVAFVPFAARWPFETWILPKRH 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 306 VLTLDQLNDEERWDLASMYSHLLKRGNAFFDkgdgkgmDLPYIAAWHQAPIHDARRENYRLNLQFFSFRRAANKIKYLAG 385
Cdd:COG1085  237 VSDFEELTDEERDDLARILKRVLRRLDNLLG-------DFPYNMGLHQAPVDGEERDHYHWHLEIYPRLRSATVLKFLAG 309
                        330       340
                 ....*....|....*....|....*..
gi 494112963 386 SESGMAAWISDTTPELIAKRFHELGSI 412
Cdd:COG1085  310 FELGAGAFINDVTPEQAAERLREVSEV 336
PRK11720 PRK11720
UDP-glucose--hexose-1-phosphate uridylyltransferase;
70-412 2.73e-53

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


Pssm-ID: 236963 [Multi-domain]  Cd Length: 346  Bit Score: 180.88  E-value: 2.73e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  70 PYAAPQMRRDPLTGDWIPMATARMNRPITAGPGATAKgNPLAARK------PGDPYQDGEVpDTDY-NVVVFENRFPS-M 141
Cdd:PRK11720   6 PVDHPHRRYNPLTGQWVLVSPHRAKRPWQGQQETPAK-ETLPAYDpdcflcPGNTRVTGDV-NPDYtGTYVFTNDFAAlM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 142 VRVPGVSEDVtyvdgNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFpfENHGQ 221
Cdd:PRK11720  84 PDTPDAPESD-----DPLFRCQSARGTSRVICFSPDHSKTLPELSVAALREVVDTWQEQTAELGKTYPWVQVF--ENKGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 222 EIGVSLAHPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVA 301
Cdd:PRK11720 157 AMGCSNPHPHGQIWANSFLPNEAEREDRLQRAYFAEHGSPLLVDYVQRELADGERIVVETEHWLAVVPYWAAWPFETLLL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 302 PVRDVLTLDQLNDEERWDLASMYSHLLKRGNAFFDkgdgkgMDLPYIAAWHQAPIHDARRENYRLNLQFF-SFRRAANKI 380
Cdd:PRK11720 237 PKAHVLRLTDLTDAQRDDLALALKKLTSRYDNLFQ------CSFPYSMGWHGAPFNGEENDHWQLHAHFYpPLLRSATVR 310
                        330       340       350
                 ....*....|....*....|....*....|..
gi 494112963 381 KYLAGSESgMAAWISDTTPELIAKRFHELGSI 412
Cdd:PRK11720 311 KFMVGYEM-LAETQRDLTAEQAAERLRAVSDI 341
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
70-412 1.92e-47

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: 165.52  E-value: 1.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963   70 PYAAPQMRRDPLTGDWIPMATARMNRPITAGPGATAKG-----NPLAARKPGDPYQDGEVpDTDY-NVVVFENRFPS-MV 142
Cdd:TIGR00209   6 PVDHPHRRYNPLTDQWILVSPHRAKRPWQGQQETPAKQvlpayDPDCYLCPGNKRVTGDL-NPDYtGTYVFTNDFAAlMS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  143 RVPGVSEDvtyvdGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFpfENHGQE 222
Cdd:TIGR00209  85 DTPDAPES-----HDPLMRCQSARGTSRVICFSPDHSKTLPELSVAALTEIVKTWQEQTAELGKTYPWVQIF--ENKGAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  223 IGVSLAHPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAP 302
Cdd:TIGR00209 158 MGCSNPHPHGQIWANSFLPNEVEREDRLQKEYFAEHKSPMLVDYVKRELADKSRTVVETEHWIAVVPYWAIWPFETLLLP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  303 VRDVLTLDQLNDEERWDLASMYSHLLKRGNAFFDkgdgkgMDLPYIAAWHQAPIHDARRENYRLNLQFF-SFRRAANKIK 381
Cdd:TIGR00209 238 KAHVLRITDLTDAQRSDLALILKKLTSKYDNLFE------TSFPYSMGWHGAPFNGEENQHWQLHAHFYpPLLRSATVRK 311
                         330       340       350
                  ....*....|....*....|....*....|.
gi 494112963  382 YLAGSESgMAAWISDTTPELIAKRFHELGSI 412
Cdd:TIGR00209 312 FMVGYEM-LGETQRDLTAEQAAERLRALSDI 341
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
73-240 1.24e-34

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: 126.64  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963   73 APQMRRDPLTGDWIPMATARMNRPItAGPGATAKGNPLAARKPGD-----PYQDGEVPDTDY-NVVVFENRFPSmvrvpg 146
Cdd:pfam01087  10 LSHRRYNPLTGEWVLVSPHRLKRPW-AGQQEKISKDTLPEYDPMCylcpgPSRANGDFNPDYkSPFVFTNDFYA------ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  147 VSEDVTYV-----DGNPLWEKKLAAGRCEVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIEQIFPFENHGQ 221
Cdd:pfam01087  83 LSKDNPYIktdaiAKNILFKAETVYGDCEVTCFLSKPELTLPLMSPKDPKAIAAAWQEKYAELGASSYPKCVLCFENEGY 162
                         170
                  ....*....|....*....
gi 494112963  222 EIGVSLAHPHGQVYCYPFI 240
Cdd:pfam01087 163 AMGCSNPHPHGQIWASSHL 181
PLN02643 PLN02643
ADP-glucose phosphorylase
74-409 2.80e-26

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 108.31  E-value: 2.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  74 PQMRRDPLTGDWIPMATARMNRPitAGPGATAKGNPLAARKPGDPYQDG--------------EVPDTDYNVVVFENRFP 139
Cdd:PLN02643   2 AELRKDPVTNRWVIFSPARGKRP--TDFKSKSPQNPNGNHSSGCPFCIGhehecapeifrvpdDASAPDWKVRVIENLYP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 140 SmvrvpgVSEDVtyvDGNPLWEKKLAAGRC--------EVICFDPNEDGLPADLPVSRLRTVVEAWAFRTAEISKMEGIE 211
Cdd:PLN02643  80 A------LSRDL---EPPCTEGQGEDYGGRrlpgfgfhDVVIETPVHSVQLSDLPARHIGEVLKAYKKRINQLQSDSRFK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 212 QIFPFENHGQEIGVSLAHPHGQVYCYPFIAPKMEKELQHTEAYHEKTGGNLLKDIMNAELeagerIVMRNHSWVAYVPAA 291
Cdd:PLN02643 151 YVQVFKNHGASAGASMSHSHSQIIALPVVPPSVSARLDGSKEYFEKTGKCSLCEVVKKDL-----LIDESSHFVSIAPFA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963 292 ARWPLEVHVAPVRDVLTLDQLNDEERWDLASMYSHLLKRGNAFFDkgdgkgmDLPYIAAWHQAPIhdaRRENYrlNLQFF 371
Cdd:PLN02643 226 ATFPFEIWIIPRDHSSNFHEIDDDKAVDLGGLLKLMLQKISKQLN-------DPPYNYMIQTSPL---GVEES--NLPYT 293
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 494112963 372 S-FRRAANKIKYLAGSESGMAAWISDTTPELIAKRFHEL 409
Cdd:PLN02643 294 HwFLQIVPQLSGVGGFELGTGCYINPVFPEDAAKVLREV 332
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
247-412 5.39e-17

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: 77.90  E-value: 5.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  247 ELQHTEAYHEKTGGNLLKDIMNAELEAGERIVMRNHSWVAYVPAAARWPLEVHVAPVRDVLTLDQLNDEERWDLASMYSH 326
Cdd:pfam02744   1 ELRSFPKYFAGHGSILLHDYVQMELAEKERVVVENESWPVVVPYWAKWPFETLLLPKRHVPSLTELTDAEREDLAAILKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494112963  327 LL-KRGNAFfdkgdgkGMDLPYIAAWHQAPIHDARRENYRLNLQFF-SFRRAANKIKYLAGSESgMAAWISDTTPELIAK 404
Cdd:pfam02744  81 LTrRYDNLF-------ETSFPYSMGIHQAPLNAEELNHWQFHPHFYpPLLRSATVRKFMVGLEI-LGERQRDLTAEQAAE 152

                  ....*...
gi 494112963  405 RFHELGSI 412
Cdd:pfam02744 153 RLRALSEV 160
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH