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Conserved domains on  [gi|18110149|ref|NP_542445|]
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glyceraldehyde 3 phosphate dehydrogenase 2, isoform A [Drosophila melanogaster]

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 1000016)

type I glyceraldehyde-3-phosphate dehydrogenase is responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02272 super family cl30355
glyceraldehyde-3-phosphate dehydrogenase
2-328 0e+00

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 591.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    2 SKIGINGFGRIGRLVLRAAIDKG-ANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTV-AAEGGFLVVNGQKITVFSERDP 79
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTInVVDDSTLEINGKQIKVTSKRDP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   80 ANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAK 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  160 VINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405

                 ....*....
gi 18110149  320 RVIDLIKYM 328
Cdd:PLN02272 406 RVLDLIEHM 414
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
2-328 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 591.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    2 SKIGINGFGRIGRLVLRAAIDKG-ANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTV-AAEGGFLVVNGQKITVFSERDP 79
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTInVVDDSTLEINGKQIKVTSKRDP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   80 ANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAK 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  160 VINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405

                 ....*....
gi 18110149  320 RVIDLIKYM 328
Cdd:PLN02272 406 RVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
1-332 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 568.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   1 MS-KIGINGFGRIGRLVLRAAIDKGAN--VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSER 77
Cdd:COG0057   1 MTiRVAINGFGRIGRLVLRALLERGPDieVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  78 DPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADA-PMFVCGVNLDAYKPDMKVVSNASCTTNCLAP 156
Cdd:COG0057  80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 157 LAKVINDNFEIVEGLMTTVHATTATQKTVDGPsGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPN 236
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 237 VSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFG 316
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
                       330
                ....*....|....*.
gi 18110149 317 YSNRVIDLIKYMQSKD 332
Cdd:COG0057 319 YSNRMVDLAEYMAKLL 334
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
3-323 7.81e-169

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 472.15  E-value: 7.81e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149     3 KIGINGFGRIGRLVLRAAIDKGAN---VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKIT-VFSERD 78
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPGNdleVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    79 PANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADA-PMFVCGVNLDAYKPDMKVVSNASCTTNCLAPL 157
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   158 AKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKlWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGI--SLNDKFVKLISWYDNEF 315
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEW 318

                  ....*...
gi 18110149   316 GYSNRVID 323
Cdd:TIGR01534 319 GYSNRLVD 326
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
149-314 1.68e-117

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 335.96  E-value: 1.68e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 149 CTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSgKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd18126   1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLI 308
Cdd:cd18126  80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159

                ....*.
gi 18110149 309 SWYDNE 314
Cdd:cd18126 160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
4-324 1.63e-111

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 326.89  E-value: 1.63e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    4 IGINGFGRIGRLVLRAAIDK-GANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANI 82
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   83 NWaSAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAP--SADAPMFVCGVNLDAYKPDM-KVVSNASCTTNCLAPLAK 159
Cdd:NF033735  81 PW-GDGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  160 VINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318

                 ....*
gi 18110149  320 RVIDL 324
Cdd:NF033735 319 RMVDL 323
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
154-311 1.72e-87

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 259.45  E-value: 1.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   154 LAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18110149   234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWY 311
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
3-149 7.12e-77

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 232.06  E-value: 7.12e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149      3 KIGINGFGRIGRLVLRAAI-DKGANVVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPAN 81
Cdd:smart00846   2 KVGINGFGRIGRLVLRAALeRPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18110149     82 INWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADA-PMFVCGVNLDAYKPDMKVVSNASC 149
Cdd:smart00846  81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
2-328 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 591.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    2 SKIGINGFGRIGRLVLRAAIDKG-ANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTV-AAEGGFLVVNGQKITVFSERDP 79
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTInVVDDSTLEINGKQIKVTSKRDP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   80 ANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAK 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  160 VINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405

                 ....*....
gi 18110149  320 RVIDLIKYM 328
Cdd:PLN02272 406 RVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
1-332 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 568.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   1 MS-KIGINGFGRIGRLVLRAAIDKGAN--VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSER 77
Cdd:COG0057   1 MTiRVAINGFGRIGRLVLRALLERGPDieVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  78 DPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADA-PMFVCGVNLDAYKPDMKVVSNASCTTNCLAP 156
Cdd:COG0057  80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 157 LAKVINDNFEIVEGLMTTVHATTATQKTVDGPsGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPN 236
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 237 VSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFG 316
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
                       330
                ....*....|....*.
gi 18110149 317 YSNRVIDLIKYMQSKD 332
Cdd:COG0057 319 YSNRMVDLAEYMAKLL 334
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
3-332 2.17e-175

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 489.35  E-value: 2.17e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    3 KIGINGFGRIGRLVLRAAIDKG-ANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPAN 81
Cdd:PTZ00023   4 KLGINGFGRIGRLVFRAALEREdVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   82 INWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAP-SADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAKV 160
Cdd:PTZ00023  84 IPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  161 INDNFEIVEGLMTTVHATTATQKTVDGPS--GKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVS 238
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  239 VVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYS 318
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYS 323
                        330
                 ....*....|....
gi 18110149  319 NRVIDLIKYMQSKD 332
Cdd:PTZ00023 324 NRLLDLAHYITQKY 337
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
3-323 7.81e-169

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 472.15  E-value: 7.81e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149     3 KIGINGFGRIGRLVLRAAIDKGAN---VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKIT-VFSERD 78
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPGNdleVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    79 PANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADA-PMFVCGVNLDAYKPDMKVVSNASCTTNCLAPL 157
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   158 AKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKlWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGI--SLNDKFVKLISWYDNEF 315
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEW 318

                  ....*...
gi 18110149   316 GYSNRVID 323
Cdd:TIGR01534 319 GYSNRLVD 326
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
3-328 1.50e-156

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 441.85  E-value: 1.50e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    3 KIGINGFGRIGRLVLRAAIDKG-ANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGT--VAAEGGFLVVNGQKITVFSERDP 79
Cdd:PLN02358   7 RIGINGFGRIGRLVARVVLQRDdVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHelKVKDDKTLLFGEKPVTVFGIRNP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   80 ANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAK 159
Cdd:PLN02358  87 EDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  160 VINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PLN02358 167 VINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:PLN02358 247 VDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSS 326

                 ....*....
gi 18110149  320 RVIDLIKYM 328
Cdd:PLN02358 327 RVVDLIVHM 335
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
3-328 1.06e-151

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 429.15  E-value: 1.06e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    3 KIGINGFGRIGRLVLRAAIDKG-ANVVAVNDpFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPAN 81
Cdd:PRK15425   4 KVGINGFGRIGRIVFRAAQKRSdIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPAN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   82 INWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSAD-APMFVCGVNLDAYKpDMKVVSNASCTTNCLAPLAKV 160
Cdd:PRK15425  83 LKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYA-GQDIVSNASCTTNCLAPLAKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  161 INDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVV 240
Cdd:PRK15425 162 INDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  241 DLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSNR 320
Cdd:PRK15425 242 DLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNK 321

                 ....*...
gi 18110149  321 VIDLIKYM 328
Cdd:PRK15425 322 VLDLIAHI 329
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
3-332 7.15e-138

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 395.19  E-value: 7.15e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    3 KIGINGFGRIGRLVLRAAIDKG-----ANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVA--------AEGGFLVVNGQ 69
Cdd:PTZ00434   5 KVGINGFGRIGRMVFQAICDQGligteIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsvKTDDVLVVNGH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   70 KI-TVFSERDPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAP-SADAPMFVCGVNLDAYKP-DMKVVSN 146
Cdd:PTZ00434  85 RIkCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPtEHHVVSN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  147 ASCTTNCLAPLAKVI-NDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKL 225
Cdd:PTZ00434 165 ASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  226 TGMAFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLN---- 301
Cdd:PTZ00434 245 TGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpge 324
                        330       340       350
                 ....*....|....*....|....*....|.
gi 18110149  302 DKFVKLISWYDNEFGYSNRVIDLIKYMQSKD 332
Cdd:PTZ00434 325 RRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
1-331 2.22e-131

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 377.93  E-value: 2.22e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    1 MSKIGINGFGRIGRLVLRAAIDKGA-NVVAVNDPFiDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDP 79
Cdd:PRK07729   2 KTKVAINGFGRIGRMVFRKAIKESAfEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   80 ANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPM-FVCGVNLDAYKPDMK-VVSNASCTTNCLAPL 157
Cdd:PRK07729  81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLAPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  158 AKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDL-RRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGY 317
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
                        330
                 ....*....|....
gi 18110149  318 SNRVIDLIKYMQSK 331
Cdd:PRK07729 320 SCRVVDLVTLVADE 333
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
149-314 1.68e-117

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 335.96  E-value: 1.68e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 149 CTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSgKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd18126   1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLI 308
Cdd:cd18126  80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159

                ....*.
gi 18110149 309 SWYDNE 314
Cdd:cd18126 160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
4-324 1.63e-111

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 326.89  E-value: 1.63e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    4 IGINGFGRIGRLVLRAAIDK-GANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANI 82
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   83 NWaSAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAP--SADAPMFVCGVNLDAYKPDM-KVVSNASCTTNCLAPLAK 159
Cdd:NF033735  81 PW-GDGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  160 VINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318

                 ....*
gi 18110149  320 RVIDL 324
Cdd:NF033735 319 RMVDL 323
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-331 5.61e-110

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 323.40  E-value: 5.61e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    1 MSKIGINGFGRIGRLVLRAAI---DKGANVVAVNDPFiDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSER 77
Cdd:PRK07403   1 MIRVAINGFGRIGRNFLRCWLgreNSQLELVAINDTS-DPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   78 DPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAP--SADAPMFVCGVNLDAYKPDM-KVVSNASCTTNCL 154
Cdd:PRK07403  80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  155 APLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPT 234
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDL-RRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  235 PNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNE 314
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
                        330
                 ....*....|....*..
gi 18110149  315 FGYSNRVIDLIKYMQSK 331
Cdd:PRK07403 319 WGYSQRVVDLAELVARK 335
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
3-324 1.52e-103

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 309.17  E-value: 1.52e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    3 KIGINGFGRIGRLVLR---AAIDKGANVVAVNDPFiDVNYMVYLFKFDSTHGRFKGTVAAEG-GFLVVNGQKITVFSERD 78
Cdd:PLN03096  62 KVAINGFGRIGRNFLRcwhGRKDSPLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGdDAISVDGKVIKVVSDRN 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   79 PANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPS-ADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPL 157
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPF 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  158 AKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNV 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGY 317
Cdd:PLN03096 300 SVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGY 379

                 ....*..
gi 18110149  318 SNRVIDL 324
Cdd:PLN03096 380 SQRVVDL 386
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
3-331 5.26e-99

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 299.12  E-value: 5.26e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    3 KIGINGFGRIGRLVLR---AAIDKGANVVAVNDPFiDVNYMVYLFKFDSTHGRFKGTVA-AEGGFLVVNGQKITVFSERD 78
Cdd:PLN02237  77 KVAINGFGRIGRNFLRcwhGRKDSPLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   79 PANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPS--ADAPMFVCGVNLDAYKPDM-KVVSNASCTTNCLA 155
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLA 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  156 PLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTP 235
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTP 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  236 NVSVVDLTVRL-GKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNE 314
Cdd:PLN02237 315 NVSVVDLVVNVeKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNE 394
                        330
                 ....*....|....*..
gi 18110149  315 FGYSNRVIDLIKYMQSK 331
Cdd:PLN02237 395 WGYSQRVVDLAHLVAAK 411
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
3-326 1.38e-98

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 294.33  E-value: 1.38e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    3 KIGINGFGRIGRLVLRAAID-KGANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPAN 81
Cdd:PRK08955   4 KVGINGFGRIGRLALRAAWDwPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIAD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   82 INWAsaGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMF--VCGVNLDAYKPDM-KVVSNASCTTNCLAPLA 158
Cdd:PRK08955  84 TDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAPVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  159 KVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVS 238
Cdd:PRK08955 162 KVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDL-RRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  239 VVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYS 318
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320

                 ....*...
gi 18110149  319 NRVIDLIK 326
Cdd:PRK08955 321 NRTAELAR 328
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
1-329 1.24e-91

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 276.55  E-value: 1.24e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    1 MSKIGINGFGRIGRLVLRAAIDKGA----NVVAVNDpFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSE 76
Cdd:PRK13535   1 TIRVAINGFGRIGRNVLRALYESGRraeiTVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   77 RDPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSA---DAPMfVCGVNLDAYKPDMKVVSNASCTTNC 153
Cdd:PRK13535  80 RDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  154 LAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDN 313
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
                        330
                 ....*....|....*.
gi 18110149  314 EFGYSNRVIDLIKYMQ 329
Cdd:PRK13535 318 EWGFANRMLDTTLAMA 333
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
154-311 1.72e-87

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 259.45  E-value: 1.72e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   154 LAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18110149   234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWY 311
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
3-148 5.58e-86

N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467614 [Multi-domain]  Cd Length: 164  Bit Score: 255.78  E-value: 5.58e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   3 KIGINGFGRIGRLVLRAAIDK-GANVVAVNDPFIDvNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPAN 81
Cdd:cd05214   2 KVGINGFGRIGRLVFRAALERdDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18110149  82 INWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSAD-APMFVCGVNLDAYKPDMKVVSNAS 148
Cdd:cd05214  81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
149-314 9.76e-86

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467673  Cd Length: 164  Bit Score: 255.23  E-value: 9.76e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 149 CTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd18123   1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGplKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLI 308
Cdd:cd18123  81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158

                ....*.
gi 18110149 309 SWYDNE 314
Cdd:cd18123 159 QWYDNE 164
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
8-328 8.71e-84

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 261.01  E-value: 8.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    8 GFGRIGRLVLRAAIDKGAN--------VVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAA--EGGFLVVNGQKITVFSER 77
Cdd:PRK08289 134 GFGRIGRLLARLLIEKTGGgnglrlraIVVRKGSEGDLEKRASLLRRDSVHGPFNGTITVdeENNAIIANGNYIQVIYAN 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   78 DPANINWASAGAE--YIVESTGVFTTIDKASTHLKG-GAKKVIISAPS-ADAPMFVCGVNLDAYKPDMKVVSNASCTTNC 153
Cdd:PRK08289 214 SPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNA 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  154 LAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSgKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:PRK08289 294 ITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH-KGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVP 372
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAA-NGPLKGILGYTDE-EVVSTDFLSDTHSSVFDAKAGISlNDKFVKLISWY 311
Cdd:PRK08289 373 TPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIV-NGNRAVLYVWY 451
                        330
                 ....*....|....*..
gi 18110149  312 DNEFGYSNRVIDLIKYM 328
Cdd:PRK08289 452 DNEFGYSCQVVRVMEQM 468
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
3-149 7.12e-77

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 232.06  E-value: 7.12e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149      3 KIGINGFGRIGRLVLRAAI-DKGANVVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPAN 81
Cdd:smart00846   2 KVGINGFGRIGRLVLRAALeRPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18110149     82 INWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADA-PMFVCGVNLDAYKPDMKVVSNASC 149
Cdd:smart00846  81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
4-332 5.18e-60

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 195.86  E-value: 5.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149    4 IGINGFGRIGRLVLRAAI-DKGANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGT-VAAEGGFLVVNG-QKITVFSERDPA 80
Cdd:PTZ00353   5 VGINGFGPVGKAVLFASLtDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGtQKIRVSAKHDLV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   81 NINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAKV 160
Cdd:PTZ00353  85 EIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  161 INDNFEIVEGLMTTVHATTATQKT-VDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PTZ00353 165 LHEVYGVEECSYTAIHGMQPQEPIaARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149  240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDThSSVFDAKAGISLND-KFVKLISWYDNEFGYS 318
Cdd:PTZ00353 245 IDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREgEVHKMVLWFDVECYYA 323
                        330
                 ....*....|....
gi 18110149  319 NRVIDLIKYMQSKD 332
Cdd:PTZ00353 324 ARLLSLVKQLHQIH 337
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
3-101 3.06e-50

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 459648 [Multi-domain]  Cd Length: 101  Bit Score: 162.27  E-value: 3.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149     3 KIGINGFGRIGRLVLRAAID-KGANVVAVNDpFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPAN 81
Cdd:pfam00044   2 KVGINGFGRIGRLVLRAALErPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
                          90       100
                  ....*....|....*....|
gi 18110149    82 INWASAGAEYIVESTGVFTT 101
Cdd:pfam00044  81 LPWGDLGVDVVIESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
3-148 2.84e-48

N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; E4PDH (EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH family of proteins.


Pssm-ID: 467615 [Multi-domain]  Cd Length: 169  Bit Score: 159.74  E-value: 2.84e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   3 KIGINGFGRIGRLVLRAAIDKGAN----VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERD 78
Cdd:cd17892   2 RVAINGYGRIGRNVLRALYESGRRaefqVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18110149  79 PANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSA---DAPMfVCGVNLDAYKPDMKVVSNAS 148
Cdd:cd17892  81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
149-314 9.35e-47

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467686  Cd Length: 165  Bit Score: 155.65  E-value: 9.35e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 149 CTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd23937   1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLI 308
Cdd:cd23937  80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159

                ....*.
gi 18110149 309 SWYDNE 314
Cdd:cd23937 160 VWCDNE 165
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
149-314 1.22e-44

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 150.36  E-value: 1.22e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 149 CTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWrdGRGAAQNIIPASTGAAKAVGKVIPALN--GKLT 226
Cdd:cd18122   1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149 227 GMAFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVK 306
Cdd:cd18122  79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158

                ....*...
gi 18110149 307 LISWYDNE 314
Cdd:cd18122 159 VFSAVDNE 166
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
3-153 1.40e-08

N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.


Pssm-ID: 467613 [Multi-domain]  Cd Length: 109  Bit Score: 51.97  E-value: 1.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18110149   3 KIGINGFGRIGRLVLRAAIDK-GANVVAVNDPfidvnymvylfkfdsthgrfkgtvaaeggflvvngqkitvfserdpan 81
Cdd:cd05192   2 RVAINGFGRIGRIVFRAIADQdDLDVVAINDR------------------------------------------------ 33
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18110149  82 inwasagAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPS-ADAPMFVCGVNLDAYKPDMKVVSNASCTTNC 153
Cdd:cd05192  34 -------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
3-38 6.83e-03

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 37.93  E-value: 6.83e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 18110149   3 KIGINGFGRIGRLVLRAAIDKGANVVAVnDPFIDVN 38
Cdd:cd12174 137 TLGVIGLGNIGRLVANAALALGMKVIGY-DPYLSVE 171
 
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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