NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|594591567|ref|NP_001277560|]
View 

glyceraldehyde-3-phosphate dehydrogenase, testis-specific isoform 1 [Mus musculus]

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 11414602)

type I glyceraldehyde-3-phosphate dehydrogenase catalyzes the NAD-dependent oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

CATH:  3.30.360.10|3.40.50.720
EC:  1.2.1.-
Gene Ontology:  GO:0006006|GO:0006096|GO:0030554|GO:0016620
PubMed:  21895736|25286305
SCOP:  4000077

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 110-435 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: 576.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG--IRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKE 187
Cdd:COG0057    5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 188 IPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDA-PMFVMGVNEKDYNPgSMTIVSNASCTTNCLAPLAK 266
Cdd:COG0057   84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 267 VIHENFGIVEGLMTTVHSYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSV 346
Cdd:COG0057  163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 347 VDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSN 426
Cdd:COG0057  242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321


                 ....*....
gi 594591567 427 RVVDLLRYM 435
Cdd:COG0057  322 RMVDLAEYM 330
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 110-435 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: 576.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG--IRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKE 187
Cdd:COG0057    5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 188 IPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDA-PMFVMGVNEKDYNPgSMTIVSNASCTTNCLAPLAK 266
Cdd:COG0057   84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 267 VIHENFGIVEGLMTTVHSYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSV 346
Cdd:COG0057  163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 347 VDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSN 426
Cdd:COG0057  242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321


                 ....*....
gi 594591567 427 RVVDLLRYM 435
Cdd:COG0057  322 RMVDLAEYM 330
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 110-435 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 573.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG-IRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEhkngqlVVD--NLEINTYQ----- 181
Cdd:PLN02272  88 IGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTIN------VVDdsTLEINGKQikvts 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 182 CKDPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDAPMFVMGVNEKDYNPgSMTIVSNASCTTNCL 261
Cdd:PLN02272 162 KRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCL 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 262 APLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPT 341
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 342 PNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNE 421
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400

                        330
                 ....*....|....
gi 594591567 422 YGYSNRVVDLLRYM 435
Cdd:PLN02272 401 WGYSNRVLDLIEHM 414
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 109-430 3.94e-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: 485.24  E-value: 3.94e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  109 TVGINGFGRIGRLVLRVCMEKG---IRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVD-NLEINTYQCKD 184
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNgKEVISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  185 PKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPS-PDAPMFVMGVNEKDYNPGSmTIVSNASCTTNCLAP 263
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  264 LAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSkKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPN 343
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  344 VSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIA--LNDNFVKLVAWYDNE 421
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317


                  ....*....
gi 594591567  422 YGYSNRVVD 430
Cdd:TIGR01534 318 WGYSNRLVD 326
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 256-421 1.04e-123

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: 355.99  E-value: 1.04e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 256 CTTNCLAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKkDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGM 335
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK-DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 336 AFRVPTPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLV 415
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                 ....*.
gi 594591567 416 AWYDNE 421
Cdd:cd18126  160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
110-431 1.46e-117

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 346.54  E-value: 1.46e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEK-GIRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 189 PWSSiGNPYVVECTGVYLSIEAASAHISSGARRVVVTAP--SPDAPMFVMGVNEKDYNPGSMTIVSNASCTTNCLAPLAK 266
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 267 VIHENFGIVEGLMTTVHSYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSV 346
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 347 VDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSN 426
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                 ....*
gi 594591567 427 RVVDL 431
Cdd:NF033735 319 RMVDL 323
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 261-418 1.95e-94

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: 281.02  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  261 LAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVP 340
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594591567  341 TPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWY 418
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 110-256 2.05e-67

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: 211.64  E-value: 2.05e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567   110 VGINGFGRIGRLVLR-VCMEKGIRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:smart00846   3 VGINGFGRIGRLVLRaALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594591567   189 PWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDA-PMFVMGVNEKDYNPgSMTIVSNASC 256
Cdd:smart00846  82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 110-435 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: 576.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG--IRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKE 187
Cdd:COG0057    5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 188 IPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDA-PMFVMGVNEKDYNPgSMTIVSNASCTTNCLAPLAK 266
Cdd:COG0057   84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 267 VIHENFGIVEGLMTTVHSYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSV 346
Cdd:COG0057  163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 347 VDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSN 426
Cdd:COG0057  242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321


                 ....*....
gi 594591567 427 RVVDLLRYM 435
Cdd:COG0057  322 RMVDLAEYM 330
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 110-435 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 573.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG-IRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEhkngqlVVD--NLEINTYQ----- 181
Cdd:PLN02272  88 IGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTIN------VVDdsTLEINGKQikvts 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 182 CKDPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDAPMFVMGVNEKDYNPgSMTIVSNASCTTNCL 261
Cdd:PLN02272 162 KRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCL 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 262 APLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPT 341
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 342 PNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNE 421
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400

                        330
                 ....*....|....
gi 594591567 422 YGYSNRVVDLLRYM 435
Cdd:PLN02272 401 WGYSNRVLDLIEHM 414
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 109-430 3.94e-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: 485.24  E-value: 3.94e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  109 TVGINGFGRIGRLVLRVCMEKG---IRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVD-NLEINTYQCKD 184
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNgKEVISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  185 PKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPS-PDAPMFVMGVNEKDYNPGSmTIVSNASCTTNCLAP 263
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  264 LAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSkKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPN 343
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  344 VSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIA--LNDNFVKLVAWYDNE 421
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317


                  ....*....
gi 594591567  422 YGYSNRVVD 430
Cdd:TIGR01534 318 WGYSNRLVD 326
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 110-439 4.92e-169

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 477.79  E-value: 4.92e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG-IRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:PTZ00023   5 LGINGFGRIGRLVFRAALEREdVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 189 PWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAP-SPDAPMFVMGVNEKDYNPgSMTIVSNASCTTNCLAPLAKV 267
Cdd:PTZ00023  85 PWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDK-SQRIVSNASCTTNCLAPLAKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 268 IHENFGIVEGLMTTVHSYTATQKTVDGPSK--KDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVS 345
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 346 VVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYS 425
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYS 323

                        330
                 ....*....|....
gi 594591567 426 NRVVDLLRYMFSRE 439
Cdd:PTZ00023 324 NRLLDLAHYITQKY 337
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
108-435 1.60e-153

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 438.40  E-value: 1.60e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 108 LTVGINGFGRIGRLVLRVCMEKG-IRVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPK 186
Cdd:PRK15425   3 IKVGINGFGRIGRIVFRAAQKRSdIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 187 EIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPD-APMFVMGVNEKDYnpGSMTIVSNASCTTNCLAPLA 265
Cdd:PRK15425  82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY--AGQDIVSNASCTTNCLAPLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 266 KVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVS 345
Cdd:PRK15425 160 KVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 346 VVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYS 425
Cdd:PRK15425 240 VVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYS 319

                        330
                 ....*....|
gi 594591567 426 NRVVDLLRYM 435
Cdd:PRK15425 320 NKVLDLIAHI 329
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 106-435 2.72e-150

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 430.30  E-value: 2.72e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 106 RELTVGINGFGRIGRLVLRVCMEKG-IRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGN-VEHKNGQ-LVVDNLEINTYQC 182
Cdd:PLN02358   4 KKIRIGINGFGRIGRLVARVVLQRDdVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHeLKVKDDKtLLFGEKPVTVFGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 183 KDPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDAPMFVMGVNEKDYNpGSMTIVSNASCTTNCLA 262
Cdd:PLN02358  84 RNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYK-SDLDIVSNASCTTNCLA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 263 PLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTP 342
Cdd:PLN02358 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 343 NVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEY 422
Cdd:PLN02358 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322

                        330
                 ....*....|...
gi 594591567 423 GYSNRVVDLLRYM 435
Cdd:PLN02358 323 GYSSRVVDLIVHM 335
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 110-440 9.84e-141

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 406.04  E-value: 9.84e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG-IRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:PRK07729   5 VAINGFGRIGRMVFRKAIKESaFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 189 PWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDAPM-FVMGVNEKDYNPGSMTIVSNASCTTNCLAPLAKV 267
Cdd:PRK07729  84 PWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHTIISNASCTTNCLAPVVKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 268 IHENFGIVEGLMTTVHSYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSVV 347
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 348 DLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSNR 427
Cdd:PRK07729 243 DLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCR 322

                        330
                 ....*....|...
gi 594591567 428 VVDLLRYMFSREK 440
Cdd:PRK07729 323 VVDLVTLVADELA 335
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 108-439 4.94e-137

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 397.50  E-value: 4.94e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 108 LTVGINGFGRIGRLVLRVCMEKG-----IRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVV---DNLEINT 179
Cdd:PTZ00434   4 IKVGINGFGRIGRMVFQAICDQGligteIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSSPSVktdDVLVVNG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 180 YQCK------DPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAP-SPDAPMFVMGVNEKDYNPGSMTIVS 252
Cdd:PTZ00434  84 HRIKcvkaqrNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPTEHHVVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 253 NASCTTNCLAPLAKVI-HENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGK 331
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 332 LTGMAFRVPTPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALN--- 408
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpg 323

                        330       340       350
                 ....*....|....*....|....*....|..
gi 594591567 409 -DNFVKLVAWYDNEYGYSNRVVDLLRYMFSRE 439
Cdd:PTZ00434 324 eRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 256-421 1.04e-123

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: 355.99  E-value: 1.04e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 256 CTTNCLAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKkDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGM 335
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK-DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 336 AFRVPTPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLV 415
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                 ....*.
gi 594591567 416 AWYDNE 421
Cdd:cd18126  160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
110-431 1.46e-117

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 346.54  E-value: 1.46e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEK-GIRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 189 PWSSiGNPYVVECTGVYLSIEAASAHISSGARRVVVTAP--SPDAPMFVMGVNEKDYNPGSMTIVSNASCTTNCLAPLAK 266
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 267 VIHENFGIVEGLMTTVHSYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSV 346
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 347 VDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSN 426
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                 ....*
gi 594591567 427 RVVDL 431
Cdd:NF033735 319 RMVDL 323
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
110-431 1.87e-116

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 344.20  E-value: 1.87e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEK---GIRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPK 186
Cdd:PRK07403   4 VAINGFGRIGRNFLRCWLGRensQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 187 EIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAP--SPDAPMFVMGVNEKDYNPGSMTIVSNASCTTNCLAPL 264
Cdd:PRK07403  83 NLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCLAPI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 265 AKVIHENFGIVEGLMTTVHSYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNV 344
Cdd:PRK07403 163 AKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 345 SVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGY 424
Cdd:PRK07403 242 SVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGY 321


                 ....*..
gi 594591567 425 SNRVVDL 431
Cdd:PRK07403 322 SQRVVDL 328
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 107-431 6.57e-105

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 318.38  E-value: 6.57e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 107 ELTVGINGFGRIGRLVLRVCMEKG---IRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVE-HKNGQLVVDNLEINTYQC 182
Cdd:PLN02237  75 KLKVAINGFGRIGRNFLRCWHGRKdspLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSN 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 183 KDPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSP--DAPMFVMGVNEKDYNPGSMTIVSNASCTTNC 260
Cdd:PLN02237 154 RDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEDDYDHEVANIVSNASCTTNC 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 261 LAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVP 340
Cdd:PLN02237 234 LAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVP 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 341 TPNVSVVDLTCRLAKPA-SYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYD 419
Cdd:PLN02237 313 TPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYD 392

                        330
                 ....*....|..
gi 594591567 420 NEYGYSNRVVDL 431
Cdd:PLN02237 393 NEWGYSQRVVDL 404
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 110-433 5.40e-104

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 312.05  E-value: 5.40e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCME-KGIRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:PRK08955   5 VGINGFGRIGRLALRAAWDwPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 189 PWSsiGNPYVVECTGVYLSIEAASAHISSGARRVVVTAP--SPDAPMFVMGVNEKDYNPGSMTIVSNASCTTNCLAPLAK 266
Cdd:PRK08955  85 DWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPvkEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPVVK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 267 VIHENFGIVEGLMTTVHSYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSV 346
Cdd:PRK08955 163 VIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 347 VDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSN 426
Cdd:PRK08955 242 TDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYAN 321


                 ....*..
gi 594591567 427 RVVDLLR 433
Cdd:PRK08955 322 RTAELAR 328
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 107-431 4.74e-101

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 306.86  E-value: 4.74e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 107 ELTVGINGFGRIGRLVLRVCMEKG---IRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVE-HKNGQLVVDNLEINTYQC 182
Cdd:PLN03096  60 KIKVAINGFGRIGRNFLRCWHGRKdspLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSD 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 183 KDPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSP-DAPMFVMGVNEKDYNPgSMTIVSNASCTTNCL 261
Cdd:PLN03096 139 RNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKH-SDPIISNASCTTNCL 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 262 APLAKVIHENFGIVEGLMTTVHSYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPT 341
Cdd:PLN03096 218 APFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPT 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 342 PNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNE 421
Cdd:PLN03096 297 PNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNE 376

                        330
                 ....*....|
gi 594591567 422 YGYSNRVVDL 431
Cdd:PLN03096 377 WGYSQRVVDL 386
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 108-435 2.52e-96

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 292.73  E-value: 2.52e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 108 LTVGINGFGRIGRLVLRVCMEKG----IRVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCK 183
Cdd:PRK13535   2 IRVAINGFGRIGRNVLRALYESGrraeITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 184 DPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSP---DAPMfVMGVNEKDYNPGSmTIVSNASCTTNC 260
Cdd:PRK13535  81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEH-RIVSNASCTTNC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 261 LAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVP 340
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 341 TPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDN 420
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317

                        330
                 ....*....|....*
gi 594591567 421 EYGYSNRVVDLLRYM 435
Cdd:PRK13535 318 EWGFANRMLDTTLAM 332
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 261-418 1.95e-94

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: 281.02  E-value: 1.95e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  261 LAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVP 340
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594591567  341 TPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWY 418
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
E4PD_g-proteo TIGR01532
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ...
 110-430 2.11e-94

erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria 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. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 130595  Cd Length: 325  Bit Score: 287.18  E-value: 2.11e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  110 VGINGFGRIGRLVLRVCMEKG----IRVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDP 185
Cdd:TIGR01532   2 VAINGFGRIGRNVLRALYESGrraeITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  186 KEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSP---DAPMfVMGVNEKDYNpGSMTIVSNASCTTNCLA 262
Cdd:TIGR01532  81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGAsdlDATI-VYGVNQDQLR-AEHRIVSNASCTTNCIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  263 PLAKVIHENFGIVEGLMTTVHSYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTP 342
Cdd:TIGR01532 159 PVIKLLDDAYGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  343 NVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEY 422
Cdd:TIGR01532 238 NVTAIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEW 317


                  ....*...
gi 594591567  423 GYSNRVVD 430
Cdd:TIGR01532 318 GFANRMLD 325
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 256-421 3.20e-84

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: 3.20e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 256 CTTNCLAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGM 335
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 336 AFRVPTPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPlaGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLV 415
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGK--GRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158


                 ....*.
gi 594591567 416 AWYDNE 421
Cdd:cd18123  159 QWYDNE 164
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 114-435 4.33e-82

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 260.63  E-value: 4.33e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 114 GFGRIGRLVLRVCMEK-----GIRVVAV---NDPFIDPEYMVYMFKYDSTHGRYKGNVE--HKNGQLVVDNLEINTYQCK 183
Cdd:PRK08289 134 GFGRIGRLLARLLIEKtgggnGLRLRAIvvrKGSEGDLEKRASLLRRDSVHGPFNGTITvdEENNAIIANGNYIQVIYAN 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 184 DPKEIPWSS--IGNPYVVECTGVYLSIEAASAHISS-GARRVVVTAPSP-DAPMFVMGVNEKDYNPgSMTIVSNASCTTN 259
Cdd:PRK08289 214 SPEEVDYTAygINNALVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKgDIKNIVHGVNHSDITD-EDKIVSAASCTTN 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 260 CLAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDwRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRV 339
Cdd:PRK08289 293 AITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRV 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 340 PTPNVSVVDLTCRLAKPASYSAITEAVKAAA-KGPLAGILAYTEDQ-VVSTDFNGNPHSSIFDAKAGIALNDNFVkLVAW 417
Cdd:PRK08289 372 PTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAV-LYVW 450

                        330
                 ....*....|....*...
gi 594591567 418 YDNEYGYSNRVVDLLRYM 435
Cdd:PRK08289 451 YDNEFGYSCQVVRVMEQM 468
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 110-255 6.04e-78

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: 239.22  E-value: 6.04e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEK-GIRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:cd05214    3 VGINGFGRIGRLVFRAALERdDIEVVAINDLT-DDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAEL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594591567 189 PWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPD-APMFVMGVNEKDYNPgSMTIVSNAS 255
Cdd:cd05214   82 PWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDA-DDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 110-256 2.05e-67

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: 211.64  E-value: 2.05e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567   110 VGINGFGRIGRLVLR-VCMEKGIRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:smart00846   3 VGINGFGRIGRLVLRaALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 594591567   189 PWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDA-PMFVMGVNEKDYNPgSMTIVSNASC 256
Cdd:smart00846  82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 108-435 3.99e-53

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 181.23  E-value: 3.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 108 LTVGINGFGRIGRLVLRVCM-EKGIRVVAVNDPFIDPEYMVYMFKYDSTHGRYKG-NVEHKNGQLVVDNLE-INTYQCKD 184
Cdd:PTZ00353   3 ITVGINGFGPVGKAVLFASLtDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGTQkIRVSAKHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 185 PKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDAPMFVMGVNEKDYNpGSMTIVSNASCTTNCLAPL 264
Cdd:PTZ00353  83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLS-ASLPVCCAGAPIAVALAPV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 265 AKVIHENFGIVEGLMTTVHSyTATQKTVDGPSK--KDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTP 342
Cdd:PTZ00353 162 IRALHEVYGVEECSYTAIHG-MQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 343 NVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNpHSSIFDAKAGIALNDNFV-KLVAWYDNE 421
Cdd:PTZ00353 241 KGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPN-GKLCYDATSSSSSREGEVhKMVLWFDVE 319

                        330
                 ....*....|....
gi 594591567 422 YGYSNRVVDLLRYM 435
Cdd:PTZ00353 320 CYYAARLLSLVKQL 333
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 256-421 1.78e-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: 160.66  E-value: 1.78e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 256 CTTNCLAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGM 335
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 336 AFRVPTPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLV 415
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159


                 ....*.
gi 594591567 416 AWYDNE 421
Cdd:cd23937  160 VWCDNE 165
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 256-421 1.16e-46

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: 158.45  E-value: 1.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 256 CTTNCLAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWrgGRGAHQNIIPSSTGAAKAVGKVIPEL--KGKLT 333
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIgkPIKVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 334 GMAFRVPTPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVK 413
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158


                 ....*...
gi 594591567 414 LVAWYDNE 421
Cdd:cd18122  159 VFSAVDNE 166
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 110-207 2.38e-45

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: 152.64  E-value: 2.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567  110 VGINGFGRIGRLVLRVCME-KGIRVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEI 188
Cdd:pfam00044   3 VGINGFGRIGRLVLRAALErPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAEL 81

                          90
                  ....*....|....*....
gi 594591567  189 PWSSIGNPYVVECTGVYLS 207
Cdd:pfam00044  82 PWGDLGVDVVIESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 110-255 5.34e-44

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: 151.65  E-value: 5.34e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLRVCMEKG----IRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDP 185
Cdd:cd17892    3 VAINGYGRIGRNVLRALYESGrraeFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594591567 186 KEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSP---DAPMfVMGVNEKDYNPgSMTIVSNAS 255
Cdd:cd17892   82 ENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRA-EHRIVSNAS 152
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 110-260 1.72e-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: 52.36  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591567 110 VGINGFGRIGRLVLR-VCMEKGIRVVAVNDpfidpeymvymfkydsthgryKGNVehkngqlvvdnleintyqckdpkei 188
Cdd:cd05192    3 VAINGFGRIGRIVFRaIADQDDLDVVAIND---------------------RRDV------------------------- 36

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 594591567 189 pwssignpyVVECTGVYLSIEAASAHISSGARRVVVTAPSP-DAPMFVMGVNEKDYNPGSmTIVSNASCTTNC 260
Cdd:cd05192   37 ---------VIECTGSFTDDDNAEKHIKAGGKKAVITAPEKgDIPTIVVVLNELAKSAGA-TVVSNANETSYS 99
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 103-154 7.76e-06

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, 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.


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 47.68  E-value: 7.76e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 594591567 103 KPARELTVGINGFGRIGRLVLRVCMEKGIRVVAVnDPFIDPEYMVYMFKYDS 154
Cdd:cd01619  139 RELEDQTVGVVGTGKIGRAVAQRAKGFGMKVIAY-DPFRNPELEDKGVKYVS 189
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
 106-150 6.70e-05

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 44.43  E-value: 6.70e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 594591567 106 RELTVGINGFGRIGRLVlrvcMEK----GIRVVAvNDPFIDPEYMVYMF 150
Cdd:cd05299  141 RGLTLGLVGFGRIGRAV----AKRakafGFRVIA-YDPYVPDGVAALGG 184
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 104-144 1.05e-04

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. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, 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.


Pssm-ID: 240650 [Multi-domain]  Cd Length: 304  Bit Score: 43.94  E-value: 1.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 594591567 104 PAREL---TVGINGFGRIGRLVLRVCMEKGIRVVAvNDPFIDPE 144
Cdd:cd12173  132 MGVELrgkTLGIVGLGRIGREVARRARAFGMKVLA-YDPYISAE 174
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 106-144 2.44e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, 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. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 42.91  E-value: 2.44e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 594591567 106 RELTVGINGFGRIGRLVLRVCMEKGIRVVAVnDPFIDPE 144
Cdd:cd12171  146 RGKTVGIVGFGAIGRRVAKRLKAFGAEVLVY-DPYVDPE 183
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 102-144 5.17e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, 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. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 41.78  E-value: 5.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 594591567 102 QKPAREL---TVGINGFGRIGRLVLRvcMEKGIRV-VAVNDPFIDPE 144
Cdd:cd12167  142 RRGGRGLygrTVGIVGFGRIGRAVVE--LLRPFGLrVLVYDPYLPAA 186
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 109-145 5.28e-04

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: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 41.70  E-value: 5.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 594591567 109 TVGINGFGRIGRLVLRVCMEKGIRVVAvNDPFIDPEY 145
Cdd:cd12172  144 TLGIIGLGRIGKAVARRLSGFGMKVLA-YDPYPDEEF 179
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 104-144 1.05e-03

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 40.95  E-value: 1.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 594591567 104 PAREL---TVGINGFGRIGRLVLRVCMEKGIRVVAVnDPFIDPE 144
Cdd:COG0111  134 RGRELrgkTVGIVGLGRIGRAVARRLRAFGMRVLAY-DPSPKPE 176
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 101-140 1.43e-03

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, 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.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 40.59  E-value: 1.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 594591567 101 LQKPARELTVGINGFGRIGRLVLRVCMEKGIRVVaVNDPF 140
Cdd:cd12158  109 QGFSLKGKTVGIVGVGNVGSRLARRLEALGMNVL-LCDPP 147
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 106-154 4.26e-03

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, 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.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 39.06  E-value: 4.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 594591567 106 RELTVGINGFGRIGRLVLRVCMEKGIRVVAVnDPFIDPEYMVYMFKYDS 154
Cdd:cd12186  144 RDLTVGIIGTGRIGSAAAKIFKGFGAKVIAY-DPYPNPELEKFLLYYDS 191
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 109-152 4.65e-03

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, 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.


Pssm-ID: 240659  Cd Length: 328  Bit Score: 38.96  E-value: 4.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 594591567 109 TVGINGFGRIGRLVLRVCMEKGIRVVAvNDPFIDPEYMVYMFKY 152
Cdd:cd12183  146 TVGVIGTGKIGQAFARILKGFGCRVLA-YDPYPNPELAKLGVEY 188
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 104-144 8.59e-03

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 37.09  E-value: 8.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 594591567  104 PAREL---TVGINGFGRIGRLVLRVCMEKGIRVVAVnDPFIDPE 144
Cdd:pfam02826  30 LGRELsgkTVGIIGLGRIGRAVAKRLKAFGMKVIAY-DRYPKPE 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH