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Conserved domains on  [gi|117676389|ref|NP_083606|]
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fucose-1-phosphate guanylyltransferase [Mus musculus]

Protein Classification

Fucokinase domain-containing protein( domain architecture ID 12085198)

Fucokinase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
 106-524 0e+00

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


:

Pssm-ID: 462323  Cd Length: 405  Bit Score: 533.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  106 SGGYSQRLPNASALGKIFTALPL---GEPIYQMLELKLAMYVDFPSNMRPGVLVTCADDIELYSVGDseyIAFDQPGFTA 182
Cdd:pfam07959   1 AGGYSQRLPSASALGKIFTALPLedpGGPVYQLLDLKLAIYSDFPSRMKPGVLVCSTDVILLFDANE---ISFDKPGVTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  183 LAHPSSLAVGTTHGVFVLHSDSSlQHGDLEYRQCYQFLHKPTIENMHRFNAVHRQrsfgqqnlsggdtdclplhtEYVYT 262
Cdd:pfam07959  78 LAHPSSLAIGTNHGVFVLDPQGS-SEKDLEIGLCRDFLHKPSEEELQASGAVLKD--------------------GFVYL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  263 DS-LFYMDHKSAKKLLDFYKSEGPLNCE-------IDAYGDFLQALGPGATAEYTRNTSHVTKEESQLLDMRQKIFHLLK 334
Cdd:pfam07959 137 DSgIVFFDGKTAEKLLALYVSPGPLDCEtylgplqIDLYGDFLQALGPGATLEYFLNTANVGKEEASLRPAREELWKLLR 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  335 GTPLNVVVLNNSRFYHIGTLQEYLLHFTSDSALKTELGLQSIAFSVSPSVPERSSGtACVIHSIVDSGCCVAPGSVVEYS 414
Cdd:pfam07959 217 GTPLNVICLPNSKFYHFGTTAEYLEHLTGDCSLRVELGLTSTAFSVIANARQLKAG-ASVINSVLEPGVSVGPGSVIEYC 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  415 RLGPEVSIGENCIISSSVIAKT----VVPAYSFLCSLSVKINGHLKYSTMVFGMQDNLKNSVktleDIKALQFFGVCFLS 490
Cdd:pfam07959 296 HLGGPVSIGSGCILSGLDLSSSlarlELPDDTFLHTLPLKLGGGKLYVTVVFGIHDNLKSSV----SDGNLTFLGKPLED 371

                         410       420       430
                  ....*....|....*....|....*....|....
gi 117676389  491 CLDIWNLKATEKLFSGNKMNLSLWTACIFPVCSS 524
Cdd:pfam07959 372 FLSLTGIQPEDLWFSGEPREKSLWNARLFPVCHD 405
 
Name Accession Description Interval E-value
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
 106-524 0e+00

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


Pssm-ID: 462323  Cd Length: 405  Bit Score: 533.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  106 SGGYSQRLPNASALGKIFTALPL---GEPIYQMLELKLAMYVDFPSNMRPGVLVTCADDIELYSVGDseyIAFDQPGFTA 182
Cdd:pfam07959   1 AGGYSQRLPSASALGKIFTALPLedpGGPVYQLLDLKLAIYSDFPSRMKPGVLVCSTDVILLFDANE---ISFDKPGVTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  183 LAHPSSLAVGTTHGVFVLHSDSSlQHGDLEYRQCYQFLHKPTIENMHRFNAVHRQrsfgqqnlsggdtdclplhtEYVYT 262
Cdd:pfam07959  78 LAHPSSLAIGTNHGVFVLDPQGS-SEKDLEIGLCRDFLHKPSEEELQASGAVLKD--------------------GFVYL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  263 DS-LFYMDHKSAKKLLDFYKSEGPLNCE-------IDAYGDFLQALGPGATAEYTRNTSHVTKEESQLLDMRQKIFHLLK 334
Cdd:pfam07959 137 DSgIVFFDGKTAEKLLALYVSPGPLDCEtylgplqIDLYGDFLQALGPGATLEYFLNTANVGKEEASLRPAREELWKLLR 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  335 GTPLNVVVLNNSRFYHIGTLQEYLLHFTSDSALKTELGLQSIAFSVSPSVPERSSGtACVIHSIVDSGCCVAPGSVVEYS 414
Cdd:pfam07959 217 GTPLNVICLPNSKFYHFGTTAEYLEHLTGDCSLRVELGLTSTAFSVIANARQLKAG-ASVINSVLEPGVSVGPGSVIEYC 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  415 RLGPEVSIGENCIISSSVIAKT----VVPAYSFLCSLSVKINGHLKYSTMVFGMQDNLKNSVktleDIKALQFFGVCFLS 490
Cdd:pfam07959 296 HLGGPVSIGSGCILSGLDLSSSlarlELPDDTFLHTLPLKLGGGKLYVTVVFGIHDNLKSSV----SDGNLTFLGKPLED 371

                         410       420       430
                  ....*....|....*....|....*....|....
gi 117676389  491 CLDIWNLKATEKLFSGNKMNLSLWTACIFPVCSS 524
Cdd:pfam07959 372 FLSLTGIQPEDLWFSGEPREKSLWNARLFPVCHD 405
fkp PRK13412
bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
 63-572 8.99e-26

bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional


Pssm-ID: 237379 [Multi-domain]  Cd Length: 974  Bit Score: 112.62  E-value: 8.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  63 QYHVFPDPAGTKIGNGGST------LCSLECLESLCGDKWNSLKVLLIHSGGYSQRLPNASALGKIFTALPL-----GEP 131
Cdd:PRK13412  50 EWFCTSDPVGQKLGSGGGTtwlleaCFRNGSPGGDFTEWLGKEKRILLHAGGQSRRLPGYAPSGKILTPVPVfrwerGQR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 132 IYQ-MLELKLAMYVDFpSNMRPGVLVTcaddieLYSVGDSeYIAFDQP----------GFTALAHPSslaVGTTHGVFVl 200
Cdd:PRK13412 130 LSQnLLSLQLPLYERI-MSKAPEGLHT------LIASGDV-YIRSEQPlqdipeadvvCYGLWVDPS---LATNHGVFV- 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 201 hsdSSLQHGDleyrQCYQFLHKPTIENMHRFnavhrqrsfgqqnlsggdtdclpLHTEYVYTD-SLFYMDHKSAKKLLDF 279
Cdd:PRK13412 198 ---SSRKSPE----RLDFMLQKPSLEELGGL-----------------------SKTHLFLMDiGIWLLSDRAVELLMKR 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 280 -YKSEGPLNCEIDAYGDFLQALGpgataeytrntSHVTKEESQLLDMRQKIFHLLKGtplnvvvlnnsRFYHIGTLQEYl 358
Cdd:PRK13412 248 sGKEDGGKLKYYDLYSDFGLALG-----------THPRIGDDELNALSVAILPLPGG-----------EFYHYGTSREL- 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 359 lhftsdsaLKTELGLQSIaFSVSPSVPERSSG---TACVIHSIVDSGCCVAPGSVV-EYSRLGPEVSIGENCIIsssvia 434
Cdd:PRK13412 305 --------ISSTLAVQNL-VTDQRRIMHRKVKphpAMFVQNAVLSGKLTAENATLWiENSHVGEGWKLASRSII------ 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 435 kTVVPAYSFLCSL--SVKIN----GHLKYSTMVFGMQDNLKNSvktLEDIKALqFFGVCFLSCLDIWNLKATEKLfsgnK 508
Cdd:PRK13412 370 -TGVPENSWNLDLpeGVCIDvvpvGDRGFVARPYGLDDVFKGA---LADGKTT-WFGRPFLEWMEARGLSWPDLK----G 440

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117676389 509 MNLSLWTACIFPVCSSLSESATASLGMLSAVRNHSPFNL-SDFNLLSIQEMLVYKDVQDMLAYRE 572
Cdd:PRK13412 441 RTDDLQAAHLFPVVTSVEELGAVLRWMLSEPSLEEGKEIwLRSEKLSADEISAYANLARLYAQRE 505
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 392-438 1.13e-05

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 44.38  E-value: 1.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 117676389 392 ACVIHSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:cd04651   24 GTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVV 70
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 389-438 9.14e-05

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 45.07  E-value: 9.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 117676389 389 SGTacVIHSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:COG0448  298 SGT--VENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVV 345
 
Name Accession Description Interval E-value
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
 106-524 0e+00

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


Pssm-ID: 462323  Cd Length: 405  Bit Score: 533.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  106 SGGYSQRLPNASALGKIFTALPL---GEPIYQMLELKLAMYVDFPSNMRPGVLVTCADDIELYSVGDseyIAFDQPGFTA 182
Cdd:pfam07959   1 AGGYSQRLPSASALGKIFTALPLedpGGPVYQLLDLKLAIYSDFPSRMKPGVLVCSTDVILLFDANE---ISFDKPGVTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  183 LAHPSSLAVGTTHGVFVLHSDSSlQHGDLEYRQCYQFLHKPTIENMHRFNAVHRQrsfgqqnlsggdtdclplhtEYVYT 262
Cdd:pfam07959  78 LAHPSSLAIGTNHGVFVLDPQGS-SEKDLEIGLCRDFLHKPSEEELQASGAVLKD--------------------GFVYL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  263 DS-LFYMDHKSAKKLLDFYKSEGPLNCE-------IDAYGDFLQALGPGATAEYTRNTSHVTKEESQLLDMRQKIFHLLK 334
Cdd:pfam07959 137 DSgIVFFDGKTAEKLLALYVSPGPLDCEtylgplqIDLYGDFLQALGPGATLEYFLNTANVGKEEASLRPAREELWKLLR 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  335 GTPLNVVVLNNSRFYHIGTLQEYLLHFTSDSALKTELGLQSIAFSVSPSVPERSSGtACVIHSIVDSGCCVAPGSVVEYS 414
Cdd:pfam07959 217 GTPLNVICLPNSKFYHFGTTAEYLEHLTGDCSLRVELGLTSTAFSVIANARQLKAG-ASVINSVLEPGVSVGPGSVIEYC 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  415 RLGPEVSIGENCIISSSVIAKT----VVPAYSFLCSLSVKINGHLKYSTMVFGMQDNLKNSVktleDIKALQFFGVCFLS 490
Cdd:pfam07959 296 HLGGPVSIGSGCILSGLDLSSSlarlELPDDTFLHTLPLKLGGGKLYVTVVFGIHDNLKSSV----SDGNLTFLGKPLED 371

                         410       420       430
                  ....*....|....*....|....*....|....
gi 117676389  491 CLDIWNLKATEKLFSGNKMNLSLWTACIFPVCSS 524
Cdd:pfam07959 372 FLSLTGIQPEDLWFSGEPREKSLWNARLFPVCHD 405
fkp PRK13412
bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
 63-572 8.99e-26

bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional


Pssm-ID: 237379 [Multi-domain]  Cd Length: 974  Bit Score: 112.62  E-value: 8.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389  63 QYHVFPDPAGTKIGNGGST------LCSLECLESLCGDKWNSLKVLLIHSGGYSQRLPNASALGKIFTALPL-----GEP 131
Cdd:PRK13412  50 EWFCTSDPVGQKLGSGGGTtwlleaCFRNGSPGGDFTEWLGKEKRILLHAGGQSRRLPGYAPSGKILTPVPVfrwerGQR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 132 IYQ-MLELKLAMYVDFpSNMRPGVLVTcaddieLYSVGDSeYIAFDQP----------GFTALAHPSslaVGTTHGVFVl 200
Cdd:PRK13412 130 LSQnLLSLQLPLYERI-MSKAPEGLHT------LIASGDV-YIRSEQPlqdipeadvvCYGLWVDPS---LATNHGVFV- 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 201 hsdSSLQHGDleyrQCYQFLHKPTIENMHRFnavhrqrsfgqqnlsggdtdclpLHTEYVYTD-SLFYMDHKSAKKLLDF 279
Cdd:PRK13412 198 ---SSRKSPE----RLDFMLQKPSLEELGGL-----------------------SKTHLFLMDiGIWLLSDRAVELLMKR 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 280 -YKSEGPLNCEIDAYGDFLQALGpgataeytrntSHVTKEESQLLDMRQKIFHLLKGtplnvvvlnnsRFYHIGTLQEYl 358
Cdd:PRK13412 248 sGKEDGGKLKYYDLYSDFGLALG-----------THPRIGDDELNALSVAILPLPGG-----------EFYHYGTSREL- 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 359 lhftsdsaLKTELGLQSIaFSVSPSVPERSSG---TACVIHSIVDSGCCVAPGSVV-EYSRLGPEVSIGENCIIsssvia 434
Cdd:PRK13412 305 --------ISSTLAVQNL-VTDQRRIMHRKVKphpAMFVQNAVLSGKLTAENATLWiENSHVGEGWKLASRSII------ 369

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676389 435 kTVVPAYSFLCSL--SVKIN----GHLKYSTMVFGMQDNLKNSvktLEDIKALqFFGVCFLSCLDIWNLKATEKLfsgnK 508
Cdd:PRK13412 370 -TGVPENSWNLDLpeGVCIDvvpvGDRGFVARPYGLDDVFKGA---LADGKTT-WFGRPFLEWMEARGLSWPDLK----G 440

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 117676389 509 MNLSLWTACIFPVCSSLSESATASLGMLSAVRNHSPFNL-SDFNLLSIQEMLVYKDVQDMLAYRE 572
Cdd:PRK13412 441 RTDDLQAAHLFPVVTSVEELGAVLRWMLSEPSLEEGKEIwLRSEKLSADEISAYANLARLYAQRE 505
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 392-438 1.13e-05

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 44.38  E-value: 1.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 117676389 392 ACVIHSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:cd04651   24 GTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVV 70
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 390-438 1.63e-05

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 43.38  E-value: 1.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 117676389 390 GTACVI-HSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:cd03356    9 GENAIIkNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAV 58
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 385-433 6.58e-05

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 42.07  E-value: 6.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 117676389 385 PERSSGTACVIHSIVDSGCCVApGSVVEYSRLGPEVSIGENCIISSSVI 433
Cdd:cd04651    1 PPYIGRRGEVKNSLVSEGCIIS-GGTVENSVLFRGVRVGSGSVVEDSVI 48
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 389-438 9.14e-05

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 45.07  E-value: 9.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 117676389 389 SGTacVIHSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:COG0448  298 SGT--VENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVV 345
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 389-438 6.82e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 42.52  E-value: 6.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 117676389 389 SGtACVIHSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:PRK00725 337 SG-AVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCV 385
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 391-454 8.87e-04

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 40.93  E-value: 8.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 117676389 391 TACV-IHSIVDSGCCVAPGSVVeysrlGPEVSIGENCII-SSSVIA-KTVVPAYSFLCSlSVKINGH 454
Cdd:cd03360   90 SAVVsPSAVIGEGCVIMAGAVI-----NPDARIGDNVIInTGAVIGhDCVIGDFVHIAP-GVVLSGG 150
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 394-438 2.11e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 40.62  E-value: 2.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 117676389 394 VIHSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:PRK05293 306 VEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAV 350
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 378-433 2.15e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 40.62  E-value: 2.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 117676389 378 FSVSPSVPERSSG-TACVIHSIVDSGCCVApGSvVEYSRLGPEVSIGENCIISSSVI 433
Cdd:PRK05293 274 YSVNPNLPPQYIAeNAKVKNSLVVEGCVVY-GT-VEHSVLFQGVQVGEGSVVKDSVI 328
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 390-438 3.16e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 36.79  E-value: 3.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 117676389 390 GTACVI-HSIVDSGCCVAPGSVVEYSRLGPEVSIGENCIISSSVIAKTVV 438
Cdd:cd05787    9 GEGTTIkNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAV 58
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 393-443 6.56e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.16  E-value: 6.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 117676389 393 CVIH--SIVDSGCCVAPGSVV-EYSRLGPEVSIGENCIISSSVI--AKTVVPAYSF 443
Cdd:cd03352   20 VVIGdgVVIGPGVVIGDGVVIgDDCVIHPNVTIYEGCIIGDRVIihSGAVIGSDGF 75
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 405-442 7.14e-03

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 37.58  E-value: 7.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 117676389 405 VAPGSVVEYSRLGPEVSIGENCIISSSVI--------------AKTVVPAYS 442
Cdd:cd03359   81 IGENCVVNAAQIGSYVHIGKNCVIGRRCIikdcvkildgtvvpPDTVIPPYS 132
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 393-432 7.76e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.85  E-value: 7.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 117676389 393 CVI--HSIVDSGCCVAPGSVVeysrlGPEVSIGENCIISSSV 432
Cdd:COG1044  121 AVIgaGVVIGDGVVIGPGVVI-----GDGVVIGDDCVLHPNV 157
 
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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