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Conserved domains on  [gi|564327416|ref|XP_006228852|]
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glyceraldehyde-3-phosphate dehydrogenase, testis-specific isoform X1 [Rattus norvegicus]

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
 102-427 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: 574.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKG-VRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEhkngrlVVD--NLEIN-----VFQ 173
Cdd:PLN02272  88 IGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTIN------VVDdsTLEINgkqikVTS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 174 CKEPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPMLVMGVNEKDYNPgSMTVVSNASCTTNCL 253
Cdd:PLN02272 162 KRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCL 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 254 APLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPT 333
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 334 PNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNE 413
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400

                        330
                 ....*....|....
gi 564327416 414 YGYSHRVVDLLRYM 427
Cdd:PLN02272 401 WGYSNRVLDLIEHM 414
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 102-427 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 574.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKG-VRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEhkngrlVVD--NLEIN-----VFQ 173
Cdd:PLN02272  88 IGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTIN------VVDdsTLEINgkqikVTS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 174 CKEPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPMLVMGVNEKDYNPgSMTVVSNASCTTNCL 253
Cdd:PLN02272 162 KRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCL 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 254 APLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPT 333
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 334 PNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNE 413
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400

                        330
                 ....*....|....
gi 564327416 414 YGYSHRVVDLLRYM 427
Cdd:PLN02272 401 WGYSNRVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 102-427 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: 559.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKG--VRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKE 179
Cdd:COG0057    5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 180 IPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDA-PMLVMGVNEKDYNPgSMTVVSNASCTTNCLAPLAK 258
Cdd:COG0057   84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 259 VIHERFGIVEGLMTTVHAYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 338
Cdd:COG0057  163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 339 VDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYSH 418
Cdd:COG0057  242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321


                 ....*....
gi 564327416 419 RVVDLLRYM 427
Cdd:COG0057  322 RMVDLAEYM 330
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 101-422 7.58e-167

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: 471.38  E-value: 7.58e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  101 TVGINGFGRIGRLVLRVCMEKG---VRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVD-NLEINVFQCKE 176
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNgKEVISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  177 PKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPS-PDAPMLVMGVNEKDYNPGSmTVVSNASCTTNCLAP 255
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  256 LAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSkKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPN 335
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  336 VSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIA--LNDNFVKLVSWYDNE 413
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317


                  ....*....
gi 564327416  414 YGYSHRVVD 422
Cdd:TIGR01534 318 WGYSNRLVD 326
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 248-413 7.27e-122

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: 350.99  E-value: 7.27e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 248 CTTNCLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKkDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGM 327
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK-DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 328 AFRVPTPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLV 407
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                 ....*.
gi 564327416 408 SWYDNE 413
Cdd:cd18126  160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
102-423 1.79e-110

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 328.05  E-value: 1.79e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEK-GVRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 181 PWSSvGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPML--VMGVNEKDYNPGSMTVVSNASCTTNCLAPLAK 258
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 259 VIHERFGIVEGLMTTVHAYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 338
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 339 VDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYSH 418
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                 ....*
gi 564327416 419 RVVDL 423
Cdd:NF033735 319 RMVDL 323
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 253-410 4.41e-91

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: 272.16  E-value: 4.41e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  253 LAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 332
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564327416  333 TPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWY 410
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 102-248 1.35e-65

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: 206.63  E-value: 1.35e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416   102 VGINGFGRIGRLVLR-VCMEKGVRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:smart00846   3 VGINGFGRIGRLVLRaALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564327416   181 PWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDA-PMLVMGVNEKDYNPgSMTVVSNASC 248
Cdd:smart00846  82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 102-427 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 574.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKG-VRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEhkngrlVVD--NLEIN-----VFQ 173
Cdd:PLN02272  88 IGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTIN------VVDdsTLEINgkqikVTS 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 174 CKEPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPMLVMGVNEKDYNPgSMTVVSNASCTTNCL 253
Cdd:PLN02272 162 KRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCL 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 254 APLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPT 333
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 334 PNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNE 413
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400

                        330
                 ....*....|....
gi 564327416 414 YGYSHRVVDLLRYM 427
Cdd:PLN02272 401 WGYSNRVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 102-427 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: 559.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKG--VRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKE 179
Cdd:COG0057    5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 180 IPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDA-PMLVMGVNEKDYNPgSMTVVSNASCTTNCLAPLAK 258
Cdd:COG0057   84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 259 VIHERFGIVEGLMTTVHAYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 338
Cdd:COG0057  163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 339 VDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYSH 418
Cdd:COG0057  242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321


                 ....*....
gi 564327416 419 RVVDLLRYM 427
Cdd:COG0057  322 RMVDLAEYM 330
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 102-431 9.59e-169

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 476.63  E-value: 9.59e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKG-VRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:PTZ00023   5 LGINGFGRIGRLVFRAALEREdVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 181 PWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAP-SPDAPMLVMGVNEKDYNPgSMTVVSNASCTTNCLAPLAKV 259
Cdd:PTZ00023  85 PWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDK-SQRIVSNASCTTNCLAPLAKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 260 IHERFGIVEGLMTTVHAYTATQKTVDGPSK--KDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 337
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 338 VVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYS 417
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYS 323

                        330
                 ....*....|....
gi 564327416 418 HRVVDLLRYMFSRE 431
Cdd:PTZ00023 324 NRLLDLAHYITQKY 337
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 101-422 7.58e-167

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: 471.38  E-value: 7.58e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  101 TVGINGFGRIGRLVLRVCMEKG---VRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVD-NLEINVFQCKE 176
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNgKEVISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  177 PKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPS-PDAPMLVMGVNEKDYNPGSmTVVSNASCTTNCLAP 255
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  256 LAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSkKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPN 335
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  336 VSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIA--LNDNFVKLVSWYDNE 413
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317


                  ....*....
gi 564327416  414 YGYSHRVVD 422
Cdd:TIGR01534 318 WGYSNRLVD 326
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
100-427 1.54e-153

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 438.01  E-value: 1.54e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKG-VRVVAVNDpFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPK 178
Cdd:PRK15425   3 IKVGINGFGRIGRIVFRAAQKRSdIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 179 EIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPD-APMLVMGVNEKDYnpGSMTVVSNASCTTNCLAPLA 257
Cdd:PRK15425  82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY--AGQDIVSNASCTTNCLAPLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 258 KVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 337
Cdd:PRK15425 160 KVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 338 VVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYS 417
Cdd:PRK15425 240 VVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYS 319

                        330
                 ....*....|
gi 564327416 418 HRVVDLLRYM 427
Cdd:PRK15425 320 NKVLDLIAHI 329
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 100-427 5.10e-151

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 431.84  E-value: 5.10e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKG-VRVVAVNDPFIDPEYMVYMFKYDSTHGRYK-GTVEHKNGR-LVVDNLEINVFQCKE 176
Cdd:PLN02358   6 IRIGINGFGRIGRLVARVVLQRDdVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKtLLFGEKPVTVFGIRN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 177 PKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPMLVMGVNEKDYNpGSMTVVSNASCTTNCLAPL 256
Cdd:PLN02358  86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYK-SDLDIVSNASCTTNCLAPL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 257 AKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 336
Cdd:PLN02358 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 337 SVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGY 416
Cdd:PLN02358 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324

                        330
                 ....*....|.
gi 564327416 417 SHRVVDLLRYM 427
Cdd:PLN02358 325 SSRVVDLIVHM 335
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 102-432 3.19e-139

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 401.81  E-value: 3.19e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKG-VRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:PRK07729   5 VAINGFGRIGRMVFRKAIKESaFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 181 PWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPM-LVMGVNEKDYNPGSMTVVSNASCTTNCLAPLAKV 259
Cdd:PRK07729  84 PWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHTIISNASCTTNCLAPVVKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 260 IHERFGIVEGLMTTVHAYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVV 339
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 340 DLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYSHR 419
Cdd:PRK07729 243 DLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCR 322

                        330
                 ....*....|...
gi 564327416 420 VVDLLRYMFSREK 432
Cdd:PRK07729 323 VVDLVTLVADELA 335
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 100-431 2.39e-138

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 400.59  E-value: 2.39e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKG-----VRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVE--------HKNGRLVVDN 166
Cdd:PTZ00434   4 IKVGINGFGRIGRMVFQAICDQGligteIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsvKTDDVLVVNG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 167 LEINVFQC-KEPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAP-SPDAPMLVMGVNEKDYNPGSMTVVS 244
Cdd:PTZ00434  84 HRIKCVKAqRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPTEHHVVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 245 NASCTTNCLAPLAKVI-HERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGK 323
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 324 LTGMAFRVPTPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALN--- 400
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpg 323

                        330       340       350
                 ....*....|....*....|....*....|..
gi 564327416 401 -DNFVKLVSWYDNEYGYSHRVVDLLRYMFSRE 431
Cdd:PTZ00434 324 eRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 248-413 7.27e-122

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: 350.99  E-value: 7.27e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 248 CTTNCLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKkDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGM 327
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK-DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 328 AFRVPTPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLV 407
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                 ....*.
gi 564327416 408 SWYDNE 413
Cdd:cd18126  160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
102-423 1.79e-110

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 328.05  E-value: 1.79e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEK-GVRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 181 PWSSvGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPML--VMGVNEKDYNPGSMTVVSNASCTTNCLAPLAK 258
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 259 VIHERFGIVEGLMTTVHAYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 338
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 339 VDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYSH 418
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                 ....*
gi 564327416 419 RVVDL 423
Cdd:NF033735 319 RMVDL 323
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
102-423 4.23e-110

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 327.63  E-value: 4.23e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEK---GVRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPK 178
Cdd:PRK07403   4 VAINGFGRIGRNFLRCWLGRensQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 179 EIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAP--SPDAPMLVMGVNEKDYNPGSMTVVSNASCTTNCLAPL 256
Cdd:PRK07403  83 NLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCLAPI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 257 AKVIHERFGIVEGLMTTVHAYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 336
Cdd:PRK07403 163 AKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 337 SVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGY 416
Cdd:PRK07403 242 SVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGY 321


                 ....*..
gi 564327416 417 SHRVVDL 423
Cdd:PRK07403 322 SQRVVDL 328
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 100-423 2.28e-100

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 306.44  E-value: 2.28e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKG---VRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGTVE-HKNGRLVVDNLEINVFQCK 175
Cdd:PLN02237  76 LKVAINGFGRIGRNFLRCWHGRKdspLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNR 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 176 EPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSP--DAPMLVMGVNEKDYNPGSMTVVSNASCTTNCL 253
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEDDYDHEVANIVSNASCTTNCL 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 254 APLAKVIHERFGIVEGLMTTVHAYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPT 333
Cdd:PLN02237 235 APFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 334 PNVSVVDLTCRLAQPAsYTA--IKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYD 411
Cdd:PLN02237 314 PNVSVVDLVVNVEKKG-ITAedVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYD 392

                        330
                 ....*....|..
gi 564327416 412 NEYGYSHRVVDL 423
Cdd:PLN02237 393 NEWGYSQRVVDL 404
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 102-425 4.84e-97

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 293.95  E-value: 4.84e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCME-KGVRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:PRK08955   5 VGINGFGRIGRLALRAAWDwPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 181 PWSsvGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPML--VMGVNEKDYNPGSMTVVSNASCTTNCLAPLAK 258
Cdd:PRK08955  85 DWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIHPIVTAASCTTNCLAPVVK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 259 VIHERFGIVEGLMTTVHAYTATQKTVDGPsKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 338
Cdd:PRK08955 163 VIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 339 VDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEYGYSH 418
Cdd:PRK08955 242 TDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYAN 321


                 ....*..
gi 564327416 419 RVVDLLR 425
Cdd:PRK08955 322 RTAELAR 328
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 100-423 2.25e-96

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 294.53  E-value: 2.25e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKG---VRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGTVE-HKNGRLVVDNLEINVFQCK 175
Cdd:PLN03096  61 IKVAINGFGRIGRNFLRCWHGRKdspLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSDR 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 176 EPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSP-DAPMLVMGVNEKDYNPgSMTVVSNASCTTNCLA 254
Cdd:PLN03096 140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKH-SDPIISNASCTTNCLA 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 255 PLAKVIHERFGIVEGLMTTVHAYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTP 334
Cdd:PLN03096 219 PFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTP 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 335 NVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEY 414
Cdd:PLN03096 298 NVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEW 377


                 ....*....
gi 564327416 415 GYSHRVVDL 423
Cdd:PLN03096 378 GYSQRVVDL 386
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 253-410 4.41e-91

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: 272.16  E-value: 4.41e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  253 LAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 332
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564327416  333 TPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWY 410
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 100-427 2.11e-89

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 274.63  E-value: 2.11e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKGVR----VVAVNDpFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCK 175
Cdd:PRK13535   2 IRVAINGFGRIGRNVLRALYESGRRaeitVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 176 EPKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSP---DApMLVMGVNEKDYNPGSmTVVSNASCTTNC 252
Cdd:PRK13535  81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDA-TVVYGVNHDQLRAEH-RIVSNASCTTNC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 253 LAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 332
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 333 TPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDN 412
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317

                        330
                 ....*....|....*
gi 564327416 413 EYGYSHRVVDLLRYM 427
Cdd:PRK13535 318 EWGFANRMLDTTLAM 332
E4PD_g-proteo TIGR01532
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ...
 102-422 9.42e-89

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: 272.54  E-value: 9.42e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  102 VGINGFGRIGRLVLRVCMEKGVR----VVAVNDpFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEP 177
Cdd:TIGR01532   2 VAINGFGRIGRNVLRALYESGRRaeitVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  178 KEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSP---DApMLVMGVNEKDYNpGSMTVVSNASCTTNCLA 254
Cdd:TIGR01532  81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGAsdlDA-TIVYGVNQDQLR-AEHRIVSNASCTTNCIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  255 PLAKVIHERFGIVEGLMTTVHAYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTP 334
Cdd:TIGR01532 159 PVIKLLDDAYGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  335 NVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLVSWYDNEY 414
Cdd:TIGR01532 238 NVTAIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEW 317


                  ....*...
gi 564327416  415 GYSHRVVD 422
Cdd:TIGR01532 318 GFANRMLD 325
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 248-413 1.69e-85

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: 258.32  E-value: 1.69e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 248 CTTNCLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGM 327
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 328 AFRVPTPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPmaGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLV 407
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGK--GRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158


                 ....*.
gi 564327416 408 SWYDNE 413
Cdd:cd18123  159 QWYDNE 164
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 106-427 1.41e-81

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 259.08  E-value: 1.41e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 106 GFGRIGRLVLRVCMEK-----GVRVVAV---NDPFIDPEYMVYMFKYDSTHGRYKGTVE--HKNGRLVVDNLEINVFQCK 175
Cdd:PRK08289 134 GFGRIGRLLARLLIEKtgggnGLRLRAIvvrKGSEGDLEKRASLLRRDSVHGPFNGTITvdEENNAIIANGNYIQVIYAN 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 176 EPKEIPWSSVG--NPYVVEATGVYLSIEAASGHISS-GARRVIVTAPSP-DAPMLVMGVNEKDYNPgSMTVVSNASCTTN 251
Cdd:PRK08289 214 SPEEVDYTAYGinNALVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKgDIKNIVHGVNHSDITD-EDKIVSAASCTTN 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 252 CLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDwRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRV 331
Cdd:PRK08289 293 AITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRV 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 332 PTPNVSVVDLTCRLAQPASYTAIKEAVKAAA-KGPMAGILAYTEDQ-VVSTDFNGDSHSSIFDAKAGIALNDNFVkLVSW 409
Cdd:PRK08289 372 PTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAV-LYVW 450

                        330
                 ....*....|....*...
gi 564327416 410 YDNEYGYSHRVVDLLRYM 427
Cdd:PRK08289 451 YDNEFGYSCQVVRVMEQM 468
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 102-247 9.37e-76

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: 233.44  E-value: 9.37e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEK-GVRVVAVNDPFiDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:cd05214    3 VGINGFGRIGRLVFRAALERdDIEVVAINDLT-DDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAEL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564327416 181 PWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPD-APMLVMGVNEKDYNPgSMTVVSNAS 247
Cdd:cd05214   82 PWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDA-DDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 102-248 1.35e-65

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: 206.63  E-value: 1.35e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416   102 VGINGFGRIGRLVLR-VCMEKGVRVVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:smart00846   3 VGINGFGRIGRLVLRaALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564327416   181 PWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDA-PMLVMGVNEKDYNPgSMTVVSNASC 248
Cdd:smart00846  82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 100-427 1.84e-54

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 184.31  E-value: 1.84e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 100 LTVGINGFGRIGRLVLRVCM-EKGVRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVV--DNLEINVFQCKE 176
Cdd:PTZ00353   3 ITVGINGFGPVGKAVLFASLtDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGASIRVVGEQIVlnGTQKIRVSAKHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 177 PKEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSPDAPMLVMGVNEKDYNpGSMTVVSNASCTTNCLAPL 256
Cdd:PTZ00353  83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLS-ASLPVCCAGAPIAVALAPV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 257 AKVIHERFGIVEGLMTTVHAyTATQKTVDGPSK--KDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTP 334
Cdd:PTZ00353 162 IRALHEVYGVEECSYTAIHG-MQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 335 NVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDShSSIFDAKAGIALNDNFV-KLVSWYDNE 413
Cdd:PTZ00353 241 KGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKMVLWFDVE 319

                        330
                 ....*....|....
gi 564327416 414 YGYSHRVVDLLRYM 427
Cdd:PTZ00353 320 CYYAARLLSLVKQL 333
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 248-413 6.15e-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: 158.84  E-value: 6.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 248 CTTNCLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGPSKKDWrgGRGAHQNIIPSSTGAAKAVGKVIPELN--GKLT 325
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 326 GMAFRVPTPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVK 405
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158


                 ....*...
gi 564327416 406 LVSWYDNE 413
Cdd:cd18122  159 VFSAVDNE 166
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 248-413 5.11e-46

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: 156.42  E-value: 5.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 248 CTTNCLAPLAKVIHERFGIVEGLMTTVHAYTATQKTVDGpSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELNGKLTGM 327
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 328 AFRVPTPNVSVVDLTCRLAQPASYTAIKEAVKAAAKGPMAGILAYTEDQVVSTDFNGDSHSSIFDAKAGIALNDNFVKLV 407
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159


                 ....*.
gi 564327416 408 SWYDNE 413
Cdd:cd23937  160 VWCDNE 165
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 102-199 1.58e-44

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: 150.33  E-value: 1.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416  102 VGINGFGRIGRLVLRVCME-KGVRVVAVNDpFIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEPKEI 180
Cdd:pfam00044   3 VGINGFGRIGRLVLRAALErPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAEL 81

                          90
                  ....*....|....*....
gi 564327416  181 PWSSVGNPYVVEATGVYLS 199
Cdd:pfam00044  82 PWGDLGVDVVIESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 102-247 1.71e-41

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: 144.72  E-value: 1.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLRVCMEKGVR----VVAVNDPfIDPEYMVYMFKYDSTHGRYKGTVEHKNGRLVVDNLEINVFQCKEP 177
Cdd:cd17892    3 VAINGYGRIGRNVLRALYESGRRaefqVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564327416 178 KEIPWSSVGNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSP---DApMLVMGVNEKDYNPgSMTVVSNAS 247
Cdd:cd17892   82 ENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDA-TIVYGINQDLLRA-EHRIVSNAS 152
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 102-252 7.10e-07

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: 47.73  E-value: 7.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564327416 102 VGINGFGRIGRLVLR-VCMEKGVRVVAVNDPfidpeymvymfkydsthgrykgtvehkngrlvvdnleinvfqckepkei 180
Cdd:cd05192    3 VAINGFGRIGRIVFRaIADQDDLDVVAINDR------------------------------------------------- 33

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564327416 181 pwssvgNPYVVEATGVYLSIEAASGHISSGARRVIVTAPSP-DAPMLVMGVNEKDYNPGSmTVVSNASCTTNC 252
Cdd:cd05192   34 ------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKgDIPTIVVVLNELAKSAGA-TVVSNANETSYS 99
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 100-146 3.42e-05

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: 45.37  E-value: 3.42e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKGVRVVAVnDPFIDPEYMVYMFKYDS 146
Cdd:cd01619  144 QTVGVVGTGKIGRAVAQRAKGFGMKVIAY-DPFRNPELEDKGVKYVS 189
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 101-137 1.24e-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: 43.63  E-value: 1.24e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 564327416 101 TVGINGFGRIGRLVLRVCMEKGVRVVAvNDPFIDPEY 137
Cdd:cd12172  144 TLGIIGLGRIGKAVARRLSGFGMKVLA-YDPYPDEEF 179
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 101-136 2.28e-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: 42.79  E-value: 2.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 564327416 101 TVGINGFGRIGRLVLRVCMEKGVRVVAvNDPFIDPE 136
Cdd:cd12173  140 TLGIVGLGRIGREVARRARAFGMKVLA-YDPYISAE 174
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 100-136 3.98e-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: 42.14  E-value: 3.98e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKGVRVVAVnDPFIDPE 136
Cdd:cd12171  148 KTVGIVGFGAIGRRVAKRLKAFGAEVLVY-DPYVDPE 183
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
 100-142 5.27e-04

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: 41.73  E-value: 5.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564327416 100 LTVGINGFGRIGRLVlrvcMEK----GVRVVAvNDPFIDPEYMVYMF 142
Cdd:cd05299  143 LTLGLVGFGRIGRAV----AKRakafGFRVIA-YDPYVPDGVAALGG 184
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 100-136 5.36e-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: 5.36e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKGVRVVaVNDPFIDPE 136
Cdd:cd12167  151 RTVGIVGFGRIGRAVVELLRPFGLRVL-VYDPYLPAA 186
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 101-136 1.43e-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: 40.56  E-value: 1.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 564327416 101 TVGINGFGRIGRLVLRVCMEKGVRVVAVnDPFIDPE 136
Cdd:COG0111  142 TVGIVGLGRIGRAVARRLRAFGMRVLAY-DPSPKPE 176
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 101-144 3.33e-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: 39.35  E-value: 3.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 564327416 101 TVGINGFGRIGRLVLRVCMEKGVRVVAvNDPFIDPEYMVYMFKY 144
Cdd:cd12183  146 TVGVIGTGKIGQAFARILKGFGCRVLA-YDPYPNPELAKLGVEY 188
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 100-146 6.81e-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: 38.29  E-value: 6.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKGVRVVAVnDPFIDPEYMVYMFKYDS 146
Cdd:cd12186  146 LTVGIIGTGRIGSAAAKIFKGFGAKVIAY-DPYPNPELEKFLLYYDS 191
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 100-132 8.68e-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: 37.89  E-value: 8.68e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 564327416 100 LTVGINGFGRIGRLVLRVCMEKGVRVVaVNDPF 132
Cdd:cd12158  116 KTVGIVGVGNVGSRLARRLEALGMNVL-LCDPP 147
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 101-136 9.21e-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: 9.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 564327416  101 TVGINGFGRIGRLVLRVCMEKGVRVVAVnDPFIDPE 136
Cdd:pfam02826  38 TVGIIGLGRIGRAVAKRLKAFGMKVIAY-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.
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