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Conserved domains on  [gi|1622842128|ref|XP_028684614|]
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glyceraldehyde-3-phosphate dehydrogenase isoform X2 [Macaca mulatta]

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
2-332 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: 602.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   2 GKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKA-ENGKLVINGSPITIFQER 80
Cdd:PLN02272   84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKR 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  81 DPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:PLN02272  244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:PLN02272  324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403
                         330
                  ....*....|..
gi 1622842128 321 SNRVVDLMAHMA 332
Cdd:PLN02272  404 SNRVLDLIEHMA 415
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
2-332 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 602.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   2 GKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKA-ENGKLVINGSPITIFQER 80
Cdd:PLN02272   84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKR 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  81 DPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:PLN02272  244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:PLN02272  324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403
                         330
                  ....*....|..
gi 1622842128 321 SNRVVDLMAHMA 332
Cdd:PLN02272  404 SNRVLDLIEHMA 415
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
3-335 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: 581.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   3 KVKVGVNGFGRIGRLVTRAAFNSGK-VDIVAINDPfIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERD 81
Cdd:COG0057     2 TIRVAINGFGRIGRLVLRALLERGPdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  82 PSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:COG0057    81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:COG0057   161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:COG0057   240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
                         330
                  ....*....|....*
gi 1622842128 321 SNRVVDLMAHMASKE 335
Cdd:COG0057   320 SNRMVDLAEYMAKLL 334
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
5-326 2.11e-172

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: 481.39  E-value: 2.11e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   5 KVGVNGFGRIGRLVTRAAFNSG--KVDIVAINDPfIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPIT-IFQERD 81
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgnDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  82 PSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIA--LNDHFVKLISWYDNEF 318
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318

                  ....*...
gi 1622842128 319 GYSNRVVD 326
Cdd:TIGR01534 319 GYSNRLVD 326
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
6-327 3.07e-121

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 351.54  E-value: 3.07e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   6 VGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPSKI 85
Cdd:NF033735    1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  86 KWGDaGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAP--SADAPMFVMGVNHEKYDNSL-KIVSNASCTTNCLAPLAK 162
Cdd:NF033735   81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 163 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV 242
Cdd:NF033735  160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 243 VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN 322
Cdd:NF033735  239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318

                  ....*
gi 1622842128 323 RVVDL 327
Cdd:NF033735  319 RMVDL 323
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
152-317 6.70e-120

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: 342.13  E-value: 6.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 152 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 232 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 311
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159

                  ....*.
gi 1622842128 312 SWYDNE 317
Cdd:cd18126   160 AWYDNE 165
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
157-314 2.51e-90

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: 266.77  E-value: 2.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 157 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 236
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622842128 237 TANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWY 314
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
4-152 1.52e-82

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: 246.69  E-value: 1.52e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128    4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPfIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPS 83
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   84 KIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIVSNASC 152
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
2-332 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 602.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   2 GKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKA-ENGKLVINGSPITIFQER 80
Cdd:PLN02272   84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKR 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  81 DPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:PLN02272  244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:PLN02272  324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403
                         330
                  ....*....|..
gi 1622842128 321 SNRVVDLMAHMA 332
Cdd:PLN02272  404 SNRVLDLIEHMA 415
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
3-335 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: 581.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   3 KVKVGVNGFGRIGRLVTRAAFNSGK-VDIVAINDPfIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERD 81
Cdd:COG0057     2 TIRVAINGFGRIGRLVLRALLERGPdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  82 PSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:COG0057    81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:COG0057   161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:COG0057   240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
                         330
                  ....*....|....*
gi 1622842128 321 SNRVVDLMAHMASKE 335
Cdd:COG0057   320 SNRMVDLAEYMAKLL 334
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
4-335 0e+00

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 510.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPS 83
Cdd:PTZ00023    3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  84 KIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAP-SADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAK 162
Cdd:PTZ00023   83 AIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 163 VIHDNFGIVEGLMTTVHAITATQKTVDGPS--GKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:PTZ00023  163 VVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:PTZ00023  243 SVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGY 322
                         330
                  ....*....|....*
gi 1622842128 321 SNRVVDLMAHMASKE 335
Cdd:PTZ00023  323 SNRLLDLAHYITQKY 337
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
5-326 2.11e-172

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: 481.39  E-value: 2.11e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   5 KVGVNGFGRIGRLVTRAAFNSG--KVDIVAINDPfIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPIT-IFQERD 81
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgnDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  82 PSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIA--LNDHFVKLISWYDNEF 318
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318

                  ....*...
gi 1622842128 319 GYSNRVVD 326
Cdd:TIGR01534 319 GYSNRLVD 326
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
3-332 2.24e-163

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 459.19  E-value: 2.24e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   3 KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKF-HGTVKAENGKLVINGS-PITIFQER 80
Cdd:PLN02358    5 KIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWkHHELKVKDDKTLLFGEkPVTVFGIR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  81 DPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPL 160
Cdd:PLN02358   85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:PLN02358  165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:PLN02358  245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
                         330
                  ....*....|..
gi 1622842128 321 SNRVVDLMAHMA 332
Cdd:PLN02358  325 SSRVVDLIVHMS 336
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
4-332 5.59e-157

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 442.64  E-value: 5.59e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDpFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPS 83
Cdd:PRK15425    3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  84 KIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSAD-APMFVMGVNHEKYDNSlKIVSNASCTTNCLAPLAK 162
Cdd:PRK15425   82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 163 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV 242
Cdd:PRK15425  161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 243 VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN 322
Cdd:PRK15425  241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
                         330
                  ....*....|
gi 1622842128 323 RVVDLMAHMA 332
Cdd:PRK15425  321 KVLDLIAHIS 330
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
3-334 2.79e-138

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 395.64  E-value: 2.79e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   3 KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFiDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDP 82
Cdd:PRK07729    2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  83 SKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADAPM-FVMGVNHEKYD-NSLKIVSNASCTTNCLAPL 160
Cdd:PRK07729   81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 161 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 240
Cdd:PRK07729  161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDL-RRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 241 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 320
Cdd:PRK07729  240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
                         330
                  ....*....|....
gi 1622842128 321 SNRVVDLMAHMASK 334
Cdd:PRK07729  320 SCRVVDLVTLVADE 333
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
1-335 5.39e-132

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 380.56  E-value: 5.39e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   1 MGKVKVGVNGFGRIGRLVTRAAFNSG----KVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGK--------LV 68
Cdd:PTZ00434    1 MAPIKVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSSpsvktddvLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  69 INGSPITIFQ-ERDPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAP-SADAPMFVMGVNHEKYD-NSLK 145
Cdd:PTZ00434   81 VNGHRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 146 IVSNASCTTNCLAPLAKVI-HDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPEL 224
Cdd:PTZ00434  161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 225 NGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALN 304
Cdd:PTZ00434  241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNN 320
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1622842128 305 ----DHFVKLISWYDNEFGYSNRVVDLMAHMASKE 335
Cdd:PTZ00434  321 lpgeRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
6-327 3.07e-121

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 351.54  E-value: 3.07e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   6 VGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPSKI 85
Cdd:NF033735    1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  86 KWGDaGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAP--SADAPMFVMGVNHEKYDNSL-KIVSNASCTTNCLAPLAK 162
Cdd:NF033735   81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 163 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV 242
Cdd:NF033735  160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 243 VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN 322
Cdd:NF033735  239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318

                  ....*
gi 1622842128 323 RVVDL 327
Cdd:NF033735  319 RMVDL 323
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
152-317 6.70e-120

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: 342.13  E-value: 6.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 152 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 232 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 311
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159

                  ....*.
gi 1622842128 312 SWYDNE 317
Cdd:cd18126   160 AWYDNE 165
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
4-334 8.74e-116

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 338.42  E-value: 8.74e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAF--NSGKVDIVAINDPFiDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERD 81
Cdd:PRK07403    2 IRVAINGFGRIGRNFLRCWLgrENSQLELVAINDTS-DPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  82 PSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAP--SADAPMFVMGVNHEKYD-NSLKIVSNASCTTNCLA 158
Cdd:PRK07403   81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDhEDHNIISNASCTTNCLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 159 PLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTA 238
Cdd:PRK07403  161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDL-RRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 239 NVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEF 318
Cdd:PRK07403  240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEW 319
                         330
                  ....*....|....*.
gi 1622842128 319 GYSNRVVDLMAHMASK 334
Cdd:PRK07403  320 GYSQRVVDLAELVARK 335
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
3-328 2.08e-109

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 322.07  E-value: 2.08e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   3 KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDP 82
Cdd:PRK08955    2 TIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  83 SKIKWgdAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADAPMF--VMGVNHEKYDNSL-KIVSNASCTTNCLAP 159
Cdd:PRK08955   82 ADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 160 LAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTAN 239
Cdd:PRK08955  160 VVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDL-RRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLAN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 240 VSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFG 319
Cdd:PRK08955  239 ASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWG 318

                  ....*....
gi 1622842128 320 YSNRVVDLM 328
Cdd:PRK08955  319 YANRTAELA 327
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
3-334 2.70e-104

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 311.09  E-value: 2.70e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   3 KVKVGVNGFGRIGRLVTRA--AFNSGKVDIVAINDPFiDLNYMVYMFQYDSTHGKFHGTVKAE-NGKLVINGSPITIFQE 79
Cdd:PLN03096   60 KIKVAINGFGRIGRNFLRCwhGRKDSPLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSD 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  80 RDPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPS-ADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLA 158
Cdd:PLN03096  139 RNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLA 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 159 PLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTA 238
Cdd:PLN03096  219 PFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTP 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 239 NVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEF 318
Cdd:PLN03096  298 NVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEW 377
                         330
                  ....*....|....*.
gi 1622842128 319 GYSNRVVDLMAHMASK 334
Cdd:PLN03096  378 GYSQRVVDLADIVANK 393
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
3-334 5.21e-104

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 312.22  E-value: 5.21e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   3 KVKVGVNGFGRIGRLVTRA--AFNSGKVDIVAINDPFIDLNyMVYMFQYDSTHGKFHGTVK-AENGKLVINGSPITIFQE 79
Cdd:PLN02237   75 KLKVAINGFGRIGRNFLRCwhGRKDSPLDVVVVNDSGGVKN-ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSN 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  80 RDPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPS--ADAPMFVMGVNHEKYDNSL-KIVSNASCTTNC 156
Cdd:PLN02237  154 RDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNC 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 157 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 236
Cdd:PLN02237  234 LAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVP 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 237 TANVSVVDLTCRLEKPA-KYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYD 315
Cdd:PLN02237  313 TPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYD 392
                         330
                  ....*....|....*....
gi 1622842128 316 NEFGYSNRVVDLMAHMASK 334
Cdd:PLN02237  393 NEWGYSQRVVDLAHLVAAK 411
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
4-332 6.04e-100

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 298.12  E-value: 6.04e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGK---VDIVAINDpFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQER 80
Cdd:PRK13535    2 IRVAINGFGRIGRNVLRALYESGRraeITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  81 DPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSA---DAPMfVMGVNHEKYDNSLKIVSNASCTTNCL 157
Cdd:PRK13535   81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 158 APLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 237
Cdd:PRK13535  160 IPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 238 ANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNE 317
Cdd:PRK13535  239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 318
                         330
                  ....*....|....*
gi 1622842128 318 FGYSNRVVDLMAHMA 332
Cdd:PRK13535  319 WGFANRMLDTTLAMA 333
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
152-317 1.01e-94

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: 278.35  E-value: 1.01e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 152 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd18123     1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 232 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGplKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 311
Cdd:cd18123    81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158

                  ....*.
gi 1622842128 312 SWYDNE 317
Cdd:cd18123   159 QWYDNE 164
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
157-314 2.51e-90

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: 266.77  E-value: 2.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 157 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 236
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622842128 237 TANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWY 314
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
4-151 8.83e-90

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: 265.80  E-value: 8.83e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDlNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPS 83
Cdd:cd05214     1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622842128  84 KIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSAD-APMFVMGVNHEKYDNSLKIVSNAS 151
Cdd:cd05214    80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
10-332 3.95e-84

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 262.17  E-value: 3.95e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  10 GFGRIGRLVTRAAFN-SGKVD------IVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKA--ENGKLVINGSPITIFQER 80
Cdd:PRK08289  134 GFGRIGRLLARLLIEkTGGGNglrlraIVVRKGSEGDLEKRASLLRRDSVHGPFNGTITVdeENNAIIANGNYIQVIYAN 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  81 DPSKI---KWG--DAgaeYVVESTGVFTTTEKAGAHLQG-GAKRVIISAPS-ADAPMFVMGVNHEKYDNSLKIVSNASCT 153
Cdd:PRK08289  214 SPEEVdytAYGinNA---LVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCT 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 154 TNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGpSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAF 233
Cdd:PRK08289  291 TNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-YHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAI 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 234 RVPTANVSVVDLTCRLEKPAKYDDIKKVVKQAS-EGPLKGILGYTE-HQVVSSDFNSDTHSSTFDAGAGIALNDHFVkLI 311
Cdd:PRK08289  370 RVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDsTEVVSSDFVGSRHAGVVDSQATIVNGNRAV-LY 448
                         330       340
                  ....*....|....*....|.
gi 1622842128 312 SWYDNEFGYSNRVVDLMAHMA 332
Cdd:PRK08289  449 VWYDNEFGYSCQVVRVMEQMA 469
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
4-152 1.52e-82

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: 246.69  E-value: 1.52e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128    4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPfIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPS 83
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   84 KIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIVSNASC 152
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
4-331 3.43e-58

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 191.24  E-value: 3.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGT-VKAENGKLVINGSP-ITIFQERD 81
Cdd:PTZ00353    3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGTQkIRVSAKHD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128  82 PSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLA 161
Cdd:PTZ00353   83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 162 KVIHDNFGIVEGLMTTVHAITAtQKTVDGPS--GKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTAN 239
Cdd:PTZ00353  163 RALHEVYGVEECSYTAIHGMQP-QEPIAARSknSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 240 VSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDThSSTFDAGAGIALNDHFV-KLISWYDNEF 318
Cdd:PTZ00353  242 GCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKMVLWFDVEC 320
                         330
                  ....*....|...
gi 1622842128 319 GYSNRVVDLMAHM 331
Cdd:PTZ00353  321 YYAARLLSLVKQL 333
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
4-104 2.94e-52

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: 167.66  E-value: 2.94e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDpFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQERDPS 83
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79
                          90       100
                  ....*....|....*....|.
gi 1622842128  84 KIKWGDAGAEYVVESTGVFTT 104
Cdd:pfam00044  80 ELPWGDLGVDVVIESTGVFTT 100
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
152-317 8.67e-51

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: 166.05  E-value: 8.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 152 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd23937     1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 232 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 311
Cdd:cd23937    80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159

                  ....*.
gi 1622842128 312 SWYDNE 317
Cdd:cd23937   160 VWCDNE 165
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
4-151 6.85e-50

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: 163.98  E-value: 6.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGK---VDIVAINDPfIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGSPITIFQER 80
Cdd:cd17892     1 YRVAINGYGRIGRNVLRALYESGRraeFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEP 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622842128  81 DPSKIKWGDAGAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPSA---DAPMfVMGVNHEKYDNSLKIVSNAS 151
Cdd:cd17892    80 DPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
152-317 5.62e-47

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: 156.53  E-value: 5.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 152 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWrdGRGALQNIIPASTGAAKAVGKVIPELN--GKLT 229
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128 230 GMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVK 309
Cdd:cd18122    79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158

                  ....*...
gi 1622842128 310 LISWYDNE 317
Cdd:cd18122   159 VFSAVDNE 166
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
4-156 3.75e-11

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: 59.29  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622842128   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPfidlnymvymfqydsthgkfhgtvkaengklvingspitifqerdps 83
Cdd:cd05192     1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDR----------------------------------------------- 33
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622842128  84 kikwgdagAEYVVESTGVFTTTEKAGAHLQGGAKRVIISAPS-ADAPMFVMGVNHEKYDNSLKIVSNASCTTNC 156
Cdd:cd05192    34 --------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-39 5.54e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 37.98  E-value: 5.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622842128   1 MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFID 39
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPE 39
 
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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