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Conserved domains on  [gi|1101115127|gb|OIO73184|]
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type I glyceraldehyde-3-phosphate dehydrogenase [Zetaproteobacteria bacterium CG1_02_49_23]

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

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List of domain hits

 Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-332 0e+00

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


:

Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 605.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAVAKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERD 80
Cdd:COG0057     1 MTIRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETY-AGQNIVSAASCTTNCLAP 159
Cdd:COG0057    81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKG-DDPTIVYGVNHDDYdADHRIISNASCTTNCLAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 160 MAKVINDNFGIKRGLMTTVHAATATQKTVDGPsMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSD 239
Cdd:COG0057   160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 240 VSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEYG 319
Cdd:COG0057   239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318

                         330
                  ....*....|...
gi 1101115127 320 YTCNMMNLVRHIA 332
Cdd:COG0057   319 YSNRMVDLAEYMA 331
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-332 0e+00

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


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 605.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAVAKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERD 80
Cdd:COG0057     1 MTIRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETY-AGQNIVSAASCTTNCLAP 159
Cdd:COG0057    81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKG-DDPTIVYGVNHDDYdADHRIISNASCTTNCLAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 160 MAKVINDNFGIKRGLMTTVHAATATQKTVDGPsMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSD 239
Cdd:COG0057   160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 240 VSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEYG 319
Cdd:COG0057   239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318

                         330
                  ....*....|...
gi 1101115127 320 YTCNMMNLVRHIA 332
Cdd:COG0057   319 YSNRMVDLAEYMA 331
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 4-325 7.66e-177

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: 492.56  E-value: 7.66e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   4 KVGINGFGRIGRMVFRA-VAKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGK-TIRLTAERDP 81
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRiLEKPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  82 ANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETY-AGQNIVSAASCTTNCLAPM 160
Cdd:TIGR01534  81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKG-DVKTIVYGVNHDEYdGEERIISNASCTTNCLAPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 161 AKVINDNFGIKRGLMTTVHAATATQKTVDGPsMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSDV 240
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 241 SVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLA--LDGTFVKLVAWYDNEY 318
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318


                  ....*..
gi 1101115127 319 GYTCNMM 325
Cdd:TIGR01534 319 GYSNRLV 325
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 3-332 4.13e-176

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 494.38  E-value: 4.13e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFR-AVAKDftDMEIVGIND-LLDADYLAYMLKYDSVHGRFDGDVSV-DGNNLVVDGKTIRLTAER 79
Cdd:PLN02272   86 TKIGINGFGRIGRLVLRiATSRD--DIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  80 DPANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkeTPMFVYNVNHETY-AGQNIVSAASCTTNCLA 158
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSAD--APMFVVGVNEKTYkPNMNIVSNASCTTNCLA 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 159 PMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTS 238
Cdd:PLN02272  242 PLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTP 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 239 DVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEY 318
Cdd:PLN02272  322 NVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEW 401

                         330
                  ....*....|....
gi 1101115127 319 GYTCNMMNLVRHIA 332
Cdd:PLN02272  402 GYSNRVLDLIEHMA 415
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
5-328 6.38e-129

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 371.19  E-value: 6.38e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   5 VGINGFGRIGRMVFRAvAKDFTDMEIVGINDLL-DADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERDPAN 83
Cdd:NF033735    1 IGINGFGRIGRLALRA-LWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  84 LKWDEvGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKETPMFVYNVNHETY--AGQNIVSAASCTTNCLAPMA 161
Cdd:NF033735   80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYdpARHRIVTAASCTTNCLAPVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 162 KVINDNFGIKRGLMTTVHAATATQKTVDGPSmKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSDVS 241
Cdd:NF033735  159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 242 VVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEYGYT 321
Cdd:NF033735  238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317


                  ....*..
gi 1101115127 322 CNMMNLV 328
Cdd:NF033735  318 NRMVDLA 324
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 152-317 2.02e-115

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: 330.57  E-value: 2.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 152 CTTNCLAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSmKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGM 231
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 232 AFRVPTSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLV 311
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1101115127 312 AWYDNE 317
Cdd:cd18126   160 AWYDNE 165
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 157-314 9.13e-89

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: 262.91  E-value: 9.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 157 LAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVP 236
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101115127 237 TSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWY 314
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 3-152 6.16e-84

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: 250.16  E-value: 6.16e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127    3 IKVGINGFGRIGRMVFRAVAKDfTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERDPA 82
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALER-PDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101115127   83 NLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETYAG-QNIVSAASC 152
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKD-ADPTFVYGVNHDEYDGeDHIISNASC 149
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-332 0e+00

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


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 605.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAVAKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERD 80
Cdd:COG0057     1 MTIRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETY-AGQNIVSAASCTTNCLAP 159
Cdd:COG0057    81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKG-DDPTIVYGVNHDDYdADHRIISNASCTTNCLAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 160 MAKVINDNFGIKRGLMTTVHAATATQKTVDGPsMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSD 239
Cdd:COG0057   160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 240 VSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEYG 319
Cdd:COG0057   239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318

                         330
                  ....*....|...
gi 1101115127 320 YTCNMMNLVRHIA 332
Cdd:COG0057   319 YSNRMVDLAEYMA 331
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 4-325 7.66e-177

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: 492.56  E-value: 7.66e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   4 KVGINGFGRIGRMVFRA-VAKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGK-TIRLTAERDP 81
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRiLEKPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  82 ANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETY-AGQNIVSAASCTTNCLAPM 160
Cdd:TIGR01534  81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKG-DVKTIVYGVNHDEYdGEERIISNASCTTNCLAPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 161 AKVINDNFGIKRGLMTTVHAATATQKTVDGPsMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSDV 240
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 241 SVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLA--LDGTFVKLVAWYDNEY 318
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318


                  ....*..
gi 1101115127 319 GYTCNMM 325
Cdd:TIGR01534 319 GYSNRLV 325
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 3-332 4.13e-176

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 494.38  E-value: 4.13e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFR-AVAKDftDMEIVGIND-LLDADYLAYMLKYDSVHGRFDGDVSV-DGNNLVVDGKTIRLTAER 79
Cdd:PLN02272   86 TKIGINGFGRIGRLVLRiATSRD--DIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  80 DPANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkeTPMFVYNVNHETY-AGQNIVSAASCTTNCLA 158
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSAD--APMFVVGVNEKTYkPNMNIVSNASCTTNCLA 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 159 PMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTS 238
Cdd:PLN02272  242 PLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTP 321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 239 DVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEY 318
Cdd:PLN02272  322 NVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEW 401

                         330
                  ....*....|....
gi 1101115127 319 GYTCNMMNLVRHIA 332
Cdd:PLN02272  402 GYSNRVLDLIEHMA 415
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-332 4.37e-167

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 468.06  E-value: 4.37e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAVAKDfTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERD 80
Cdd:PRK15425    1 MTIKVGINGFGRIGRIVFRAAQKR-SDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKeTPMFVYNVNHETYAGQNIVSAASCTTNCLAPM 160
Cdd:PRK15425   80 PANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDN-TPMFVKGANFDKYAGQDIVSNASCTTNCLAPL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 161 AKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSDV 240
Cdd:PRK15425  159 AKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 241 SVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEYGY 320
Cdd:PRK15425  239 SVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGY 318

                         330
                  ....*....|..
gi 1101115127 321 TCNMMNLVRHIA 332
Cdd:PRK15425  319 SNKVLDLIAHIS 330
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-331 2.46e-157

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 443.51  E-value: 2.46e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAvAKDFTDMEIVGIND-LLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAER 79
Cdd:PTZ00023    1 MVVKLGINGFGRIGRLVFRA-ALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  80 DPANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETY-AGQNIVSAASCTTNCLA 158
Cdd:PTZ00023   80 DPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKD-DTPIYVMGVNHTQYdKSQRIVSNASCTTNCLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 159 PMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSM--KDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVP 236
Cdd:PTZ00023  159 PLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 237 TSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDN 316
Cdd:PTZ00023  239 VPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDN 318

                         330
                  ....*....|....*
gi 1101115127 317 EYGYTCNMMNLVRHI 331
Cdd:PTZ00023  319 EWGYSNRLLDLAHYI 333
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-332 1.15e-136

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 391.41  E-value: 1.15e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAVAKDfTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERD 80
Cdd:PRK07729    1 MKTKVAINGFGRIGRMVFRKAIKE-SAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETYAGQN--IVSAASCTTNCLA 158
Cdd:PRK07729   80 PKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKN-EDVTIVVGVNEDQLDIEKhtIISNASCTTNCLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 159 PMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSmKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTS 238
Cdd:PRK07729  159 PVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 239 DVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEY 318
Cdd:PRK07729  238 NVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEW 317

                         330
                  ....*....|....
gi 1101115127 319 GYTCNMMNLVRHIA 332
Cdd:PRK07729  318 GYSCRVVDLVTLVA 331
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 3-332 3.48e-129

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 372.52  E-value: 3.48e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKDfTDMEIVGIND-LLDADYLAYMLKYDSVHGRFD-GDVSV-DGNNLVVDGKTIRLTAER 79
Cdd:PLN02358    6 IRIGINGFGRIGRLVARVVLQR-DDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhHELKVkDDKTLLFGEKPVTVFGIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  80 DPANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkeTPMFVYNVN-HETYAGQNIVSAASCTTNCLA 158
Cdd:PLN02358   85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD--APMFVVGVNeHEYKSDLDIVSNASCTTNCLA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 159 PMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTS 238
Cdd:PLN02358  163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 239 DVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEY 318
Cdd:PLN02358  243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322

                         330
                  ....*....|....
gi 1101115127 319 GYTCNMMNLVRHIA 332
Cdd:PLN02358  323 GYSSRVVDLIVHMS 336
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
5-328 6.38e-129

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 371.19  E-value: 6.38e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   5 VGINGFGRIGRMVFRAvAKDFTDMEIVGINDLL-DADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERDPAN 83
Cdd:NF033735    1 IGINGFGRIGRLALRA-LWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIED 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  84 LKWDEvGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKETPMFVYNVNHETY--AGQNIVSAASCTTNCLAPMA 161
Cdd:NF033735   80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYdpARHRIVTAASCTTNCLAPVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 162 KVINDNFGIKRGLMTTVHAATATQKTVDGPSmKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSDVS 241
Cdd:NF033735  159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 242 VVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEYGYT 321
Cdd:NF033735  238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317


                  ....*..
gi 1101115127 322 CNMMNLV 328
Cdd:NF033735  318 NRMVDLA 324
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-332 1.52e-127

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 369.00  E-value: 1.52e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAVAKD---FTDMEIVGINDL-LDADYLAYMLKYDSVHGRFDGDVSV--------DGNNLVV 68
Cdd:PTZ00434    2 APIKVGINGFGRIGRMVFQAICDQgliGTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  69 DGKTIR-LTAERDPANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKeTPMFVYNVNHETYA--GQN 145
Cdd:PTZ00434   82 NGHRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGG-AKTIVMGVNQHEYSptEHH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 146 IVSAASCTTNCLAPMAKVI-NDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPEL 224
Cdd:PTZ00434  161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 225 NGKLTGMAFRVPTSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGA----G 300
Cdd:PTZ00434  241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKAtlqnN 320

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1101115127 301 LALDGTFVKLVAWYDNEYGYTCNMMNLVRHIA 332
Cdd:PTZ00434  321 LPGERRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
2-332 4.37e-121

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 351.90  E-value: 4.37e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   2 TIKVGINGFGRIGRMVFRA-VAKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERD 80
Cdd:PRK07403    1 MIRVAINGFGRIGRNFLRCwLGRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKETPMFVYNVNHETYAGQ--NIVSAASCTTNCLA 158
Cdd:PRK07403   81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEdhNIISNASCTTNCLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 159 PMAKVINDNFGIKRGLMTTVHAATATQKTVDGpSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTS 238
Cdd:PRK07403  161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 239 DVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEY 318
Cdd:PRK07403  240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEW 319

                         330
                  ....*....|....
gi 1101115127 319 GYTCNMMNLVRHIA 332
Cdd:PRK07403  320 GYSQRVVDLAELVA 333
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 152-317 2.02e-115

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: 330.57  E-value: 2.02e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 152 CTTNCLAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSmKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGM 231
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 232 AFRVPTSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLV 311
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1101115127 312 AWYDNE 317
Cdd:cd18126   160 AWYDNE 165
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-329 8.04e-113

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 330.54  E-value: 8.04e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAvAKDFTDMEIVGINDLL-DADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAER 79
Cdd:PRK08955    1 MTIKVGINGFGRIGRLALRA-AWDWPELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  80 DPANLKWDevGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKETPMFVYNVNHETY--AGQNIVSAASCTTNCL 157
Cdd:PRK08955   80 AIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFdpAIHPIVTAASCTTNCL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 158 APMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSmKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPT 237
Cdd:PRK08955  158 APVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 238 SDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNE 317
Cdd:PRK08955  237 ANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNE 316

                         330
                  ....*....|..
gi 1101115127 318 YGYTCNMMNLVR 329
Cdd:PRK08955  317 WGYANRTAELAR 328
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 3-332 1.69e-102

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 307.98  E-value: 1.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRA-VAKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVS-VDGNNLVVDGKTIRLTAERD 80
Cdd:PLN02237   76 LKVAINGFGRIGRNFLRCwHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRD 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKETPMFVYNVNHETYAGQ--NIVSAASCTTNCLA 158
Cdd:PLN02237  156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIPTYVVGVNEDDYDHEvaNIVSNASCTTNCLA 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 159 PMAKVINDNFGIKRGLMTTVHAATATQKTVDGpSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTS 238
Cdd:PLN02237  236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTP 314

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 239 DVSVVDLTCELEKE-TTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNE 317
Cdd:PLN02237  315 NVSVVDLVVNVEKKgITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNE 394

                         330
                  ....*....|....*
gi 1101115127 318 YGYTCNMMNLVRHIA 332
Cdd:PLN02237  395 WGYSQRVVDLAHLVA 409
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 3-332 2.98e-102

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 305.70  E-value: 2.98e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRAV-AKDFTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNN-LVVDGKTIRLTAERD 80
Cdd:PLN03096   61 IKVAINGFGRIGRNFLRCWhGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRN 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETYAGQN-IVSAASCTTNCLAP 159
Cdd:PLN03096  141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKG-DIPTYVVGVNADDYKHSDpIISNASCTTNCLAP 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 160 MAKVINDNFGIKRGLMTTVHAATATQKTVDGpSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPTSD 239
Cdd:PLN03096  220 FVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 240 VSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNEYG 319
Cdd:PLN03096  299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWG 378

                         330
                  ....*....|...
gi 1101115127 320 YTCNMMNLVRHIA 332
Cdd:PLN03096  379 YSQRVVDLADIVA 391
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 2-326 4.94e-94

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 282.72  E-value: 4.94e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   2 TIKVGINGFGRIGRMVFRAV---AKDfTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAE 78
Cdd:PRK13535    1 TIRVAINGFGRIGRNVLRALyesGRR-AEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  79 RDPANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKETPMFVYNVNHETY-AGQNIVSAASCTTNCL 157
Cdd:PRK13535   80 RDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLrAEHRIVSNASCTTNCI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 158 APMAKVINDNFGIKRGLMTTVHAATATQKTVDGpSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVPT 237
Cdd:PRK13535  160 IPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 238 SDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWYDNE 317
Cdd:PRK13535  239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 318


                  ....*....
gi 1101115127 318 YGYTCNMMN 326
Cdd:PRK13535  319 WGFANRMLD 327
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 157-314 9.13e-89

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: 262.91  E-value: 9.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 157 LAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMAFRVP 236
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101115127 237 TSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLVAWY 314
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 3-151 1.16e-87

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: 260.02  E-value: 1.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKDfTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERDPA 82
Cdd:cd05214     1 IKVGINGFGRIGRLVFRAALER-DDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  83 NLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETY-AGQNIVSAAS 151
Cdd:cd05214    80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKD-DDPTIVMGVNHDKYdADDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 3-152 6.16e-84

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: 250.16  E-value: 6.16e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127    3 IKVGINGFGRIGRMVFRAVAKDfTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERDPA 82
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALER-PDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101115127   83 NLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNHETYAG-QNIVSAASC 152
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKD-ADPTFVYGVNHDEYDGeDHIISNASC 149
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 9-332 5.13e-82

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 256.39  E-value: 5.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   9 GFGRIGRMVFRAVakdftdMEIVGINDLL-----------DADYL--AYMLKYDSVHGRFDGDVSVDGNN--LVVDGKTI 73
Cdd:PRK08289  134 GFGRIGRLLARLL------IEKTGGGNGLrlraivvrkgsEGDLEkrASLLRRDSVHGPFNGTITVDEENnaIIANGNYI 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  74 RLTAERDPANLKWDEVGAE--IVIDCTGFFLTTESCQAHINA-GAKKVVQSAPAKDkETPMFVYNVNHETYAGQ-NIVSA 149
Cdd:PRK08289  208 QVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKG-DIKNIVHGVNHSDITDEdKIVSA 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 150 ASCTTNCLAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDwRGGRGILENIIPSSTGAAKAVGIVLPELNGKLT 229
Cdd:PRK08289  287 ASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLT 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 230 GMAFRVPTSDVSVVDLTCELEKETTYEEICAAMKAAA-EGEMSATLGYTDDK-VVSTDFRGIRNSSIFDAGAGLAlDGTF 307
Cdd:PRK08289  366 GNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIV-NGNR 444

                         330       340
                  ....*....|....*....|....*
gi 1101115127 308 VKLVAWYDNEYGYTCNMMNLVRHIA 332
Cdd:PRK08289  445 AVLYVWYDNEFGYSCQVVRVMEQMA 469
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 152-317 7.54e-81

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: 242.91  E-value: 7.54e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 152 CTTNCLAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGM 231
Cdd:cd18123     1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 232 AFRVPTSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSatLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLV 311
Cdd:cd18123    81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGKGR--LGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158


                  ....*.
gi 1101115127 312 AWYDNE 317
Cdd:cd18123   159 QWYDNE 164
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 3-103 2.52e-57

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: 180.38  E-value: 2.52e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKDFtDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERDPA 82
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERP-DIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79

                          90       100
                  ....*....|....*....|.
gi 1101115127  83 NLKWDEVGAEIVIDCTGFFLT 103
Cdd:pfam00044  80 ELPWGDLGVDVVIESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 3-151 1.68e-52

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: 170.53  E-value: 1.68e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKD--FTDMEIVGINDLLDADYLAYMLKYDSVHGRFDGDVSVDGNNLVVDGKTIRLTAERD 80
Cdd:cd17892     1 YRVAINGYGRIGRNVLRALYESgrRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1101115127  81 PANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDKETPMFVYNVNHETYAGQN-IVSAAS 151
Cdd:cd17892    81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAEHrIVSNAS 152
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 152-317 2.55e-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: 157.30  E-value: 2.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 152 CTTNCLAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMKDWrgGRGILENIIPSSTGAAKAVGIVLPELN--GKLT 229
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 230 GMAFRVPTSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVK 309
Cdd:cd18122    79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158


                  ....*...
gi 1101115127 310 LVAWYDNE 317
Cdd:cd18122   159 VFSAVDNE 166
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-331 4.08e-47

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 162.35  E-value: 4.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   1 MTIKVGINGFGRIGRMVFRAvakDFTD--MEIVGINDL-LDADYLAYMLKYDSVHGRFDG-DVSVDGNNLVVDG-KTIRL 75
Cdd:PTZ00353    1 LPITVGINGFGPVGKAVLFA---SLTDplVTVVAVNDAsVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGtQKIRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  76 TAERDPANLKWDEVGAEIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkeTPMFVYNVNHETY-AGQNIVSAASCTT 154
Cdd:PTZ00353   78 SAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSAD--APTVMAGSNDERLsASLPVCCAGAPIA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 155 NCLAPMAKVINDNFGIKRGLMTTVHAaTATQKTVDGPSM--KDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGMA 232
Cdd:PTZ00353  156 VALAPVIRALHEVYGVEECSYTAIHG-MQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 233 FRVPTSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFrgIRNSS-IFDAGAGLAL-DGTFVKL 310
Cdd:PTZ00353  235 FQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDC--IPNGKlCYDATSSSSSrEGEVHKM 312

                         330       340
                  ....*....|....*....|.
gi 1101115127 311 VAWYDNEYGYTCNMMNLVRHI 331
Cdd:PTZ00353  313 VLWFDVECYYAARLLSLVKQL 333
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 152-317 1.69e-42

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: 144.86  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 152 CTTNCLAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGpSMKDWRGGRGILENIIPSSTGAAKAVGIVLPELNGKLTGM 231
Cdd:cd23937     1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 232 AFRVPTSDVSVVDLTCELEKETTYEEICAAMKAAAEGEMSATLGYTDDKVVSTDFRGIRNSSIFDAGAGLALDGTFVKLV 311
Cdd:cd23937    80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159


                  ....*.
gi 1101115127 312 AWYDNE 317
Cdd:cd23937   160 VWCDNE 165
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 3-156 5.41e-17

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: 75.47  E-value: 5.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKDfTDMEIVGINDLLDadylaymlkydsvhgrfdgdvsvdgnnlvvdgktirltaerdpa 82
Cdd:cd05192     1 IRVAINGFGRIGRIVFRAIADQ-DDLDVVAINDRRD-------------------------------------------- 35

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1101115127  83 nlkwdevgaeIVIDCTGFFLTTESCQAHINAGAKKVVQSAPAKDkETPMFVYNVNH-ETYAGQNIVSAASCTTNC 156
Cdd:cd05192    36 ----------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKG-DIPTIVVVLNElAKSAGATVVSNANETSYS 99
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-264 1.29e-09

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 58.69  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKDfTDMEIVGINDlLDADYLAYMLKydsvhgrfdgdvsvdgnnlvvdGKTIRLTAERDPA 82
Cdd:PRK04207    2 IKVGVNGYGTIGKRVADAVAAQ-PDMELVGVAK-TKPDYEARVAV----------------------EKGYPLYVADPER 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127  83 NLKWDEVG-------------AEIVIDCTgfflttescQAHINAGAKKVVQSAPAK-------DKETPMFVYN--VNHET 140
Cdd:PRK04207   58 EKAFEEAGipvagtiedllekADIVVDAT---------PGGVGAKNKELYEKAGVKaifqggeKAEVAGVSFNalANYEE 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 141 YAGQNIVSAASCTTNCLAPMAKVINDNFGIKRGLMTTVHAATATQKTVDGPSMkdwrggrGILENI--IPSSTGaaKAVG 218
Cdd:PRK04207  129 ALGKDYVRVVSCNTTGLCRTLCALDRAFGVKKVRATLVRRAADPKEVKRGPIN-------AIVPDPvtVPSHHG--PDVK 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1101115127 219 IVLPELNgkLTGMAFRVPTSDVSVVDLTCELEKETTYEEICAAMKA 264
Cdd:PRK04207  200 TVLPDLD--ITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEALEN 243
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 152-264 6.82e-05

C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. This family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.


Pssm-ID: 467680 [Multi-domain]  Cd Length: 180  Bit Score: 42.99  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101115127 152 CTTNCLAPMAKVINDNFGIKRGLMTTVHAAT-ATQKTVdgPSMkdwrggrGILENIIPSSTGAAKAVGIVLPELNGKLTG 230
Cdd:cd18130     1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAISgAGYPGV--PSL-------DILDNVIPYIGGEEEKIESETKKILGTLNE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1101115127 231 MAF------------RVPTSDVSVVDLTCELEKETTYEEICAAMKA 264
Cdd:cd18130    72 DKIepadfkvsatcnRVPVIDGHTESVSVKFKERPDPEEVKEALEN 117
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 3-33 2.92e-04

N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467610 [Multi-domain]  Cd Length: 151  Bit Score: 40.63  E-value: 2.92e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKDfTDMEIVGI 33
Cdd:cd02270     1 IRVAIVGYGNLGRGVEEAIQAN-PDMELVGV 30
GAPDH_II_N cd02278
N-terminal NAD(P)-binding domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 3-33 8.20e-04

N-terminal NAD(P)-binding domain of type II 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 type II NADP+ utilizing GAPDHs mainly from archaea.


Pssm-ID: 467612  Cd Length: 171  Bit Score: 39.47  E-value: 8.20e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1101115127   3 IKVGINGFGRIGRMVFRAVAKDFtDMEIVGI 33
Cdd:cd02278     1 IKVGVNGYGTIGKRVADAVLLQD-DMELVGV 30
 
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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