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Conserved domains on  [gi|222522779|gb|ACM63081|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Klebsiella sp. CRLS061a]

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 ...
 2-173 5.18e-117

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: 334.29  E-value: 5.18e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:COG0057  105 EKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTND 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:COG0057  185 QNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKE 263

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:COG0057  264 AAEGPLKGILGYT 276
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-173 5.18e-117

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: 334.29  E-value: 5.18e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:COG0057  105 EKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTND 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:COG0057  185 QNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKE 263

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:COG0057  264 AAEGPLKGILGYT 276
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-173 1.82e-116

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 332.85  E-value: 1.82e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   1 DETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETYAGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:PRK15425 103 DETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTAT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:PRK15425 183 QKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKA 262

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:PRK15425 263 AAEGEMKGVLGYT 275
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-173 1.73e-101

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: 294.57  E-value: 1.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779    1 DETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTA 79
Cdd:TIGR01534 103 KEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYdGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTN 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   80 TQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIK 159
Cdd:TIGR01534 183 DQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALK 261

                         170
                  ....*....|....
gi 222522779  160 AASEGAMKGVLGYT 173
Cdd:TIGR01534 262 EASEGELKGVLGYT 275
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 48-173 5.98e-96

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: 274.72  E-value: 5.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  48 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 127
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 222522779 128 AFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAASEGAMKGVLGYT 173
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYT 125
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 53-173 5.78e-76

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: 224.01  E-value: 5.78e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   53 LAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 132
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 222522779  133 TPNVSVVDLTVRLEKAASYEEIKKAIKAASEGAMKGVLGYT 173
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYT 121
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
2-172 4.35e-56

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 178.97  E-value: 4.35e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKD-NTPMFVRGANFETY--AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATT 78
Cdd:NF033735 100 EKLQPYFDQGVKKVVVSAPVKEeGVLNIVYGVNDHLYdpARHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDIT 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  79 ATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAI 158
Cdd:NF033735 180 NTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALF 258

                        170
                 ....*....|....
gi 222522779 159 KAASEGAMKGVLGY 172
Cdd:NF033735 259 KAAAEGPLKGILGY 272
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-173 5.18e-117

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: 334.29  E-value: 5.18e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:COG0057  105 EKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTND 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:COG0057  185 QNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKE 263

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:COG0057  264 AAEGPLKGILGYT 276
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-173 1.82e-116

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 332.85  E-value: 1.82e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   1 DETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETYAGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:PRK15425 103 DETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTAT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:PRK15425 183 QKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKA 262

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:PRK15425 263 AAEGEMKGVLGYT 275
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 2-173 6.84e-112

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 324.50  E-value: 6.84e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDnTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:PLN02272 189 EKASAHLKGGAKKVVISAPSAD-APMFVVGVNEKTYkPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTAT 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:PLN02272 268 QKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKY 347

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:PLN02272 348 ASEGPLKGILGYT 360
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-173 1.73e-101

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: 294.57  E-value: 1.73e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779    1 DETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTA 79
Cdd:TIGR01534 103 KEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYdGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTN 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   80 TQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIK 159
Cdd:TIGR01534 183 DQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALK 261

                         170
                  ....*....|....
gi 222522779  160 AASEGAMKGVLGYT 173
Cdd:TIGR01534 262 EASEGELKGVLGYT 275
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 48-173 5.98e-96

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: 274.72  E-value: 5.98e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  48 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 127
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 222522779 128 AFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAASEGAMKGVLGYT 173
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYT 125
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 2-173 1.39e-92

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 272.48  E-value: 1.39e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:PTZ00023 105 EKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYdKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTAN 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPSH--KDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAI 158
Cdd:PTZ00023 185 QLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAV 264

                        170
                 ....*....|....*
gi 222522779 159 KAASEGAMKGVLGYT 173
Cdd:PTZ00023 265 KKAAEGPLKGILGYT 279
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 2-173 5.51e-86

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 255.80  E-value: 5.51e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDnTPMFVRGANFETYAGQ-DIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:PLN02358 110 DKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEYKSDlDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITAT 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:PLN02358 189 QKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKE 268

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:PLN02358 269 ESEGKLKGILGYT 281
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-173 7.33e-78

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 235.40  E-value: 7.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   1 DETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETYAGQ--DIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATT 78
Cdd:PRK07729 103 KEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEkhTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYT 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  79 ATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAI 158
Cdd:PRK07729 183 NDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEAF 261

                        170
                 ....*....|....*
gi 222522779 159 KAASEGAMKGVLGYT 173
Cdd:PRK07729 262 KTAANGALKGILEFS 276
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 53-173 5.78e-76

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: 224.01  E-value: 5.78e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   53 LAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 132
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 222522779  133 TPNVSVVDLTVRLEKAASYEEIKKAIKAASEGAMKGVLGYT 173
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYT 121
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 4-173 3.84e-72

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 221.47  E-value: 3.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   4 ARKHITAGAKKVVLTGPSKDNTPMFVRGANFETYAGQD--IVSNASCTTNCLAPLAKVI-NDNFGIVEGLMTTVHATTAT 80
Cdd:PTZ00434 121 AEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEhhVVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTAT 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:PTZ00434 201 QKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKR 280

                        170
                 ....*....|...
gi 222522779 161 ASEGAMKGVLGYT 173
Cdd:PTZ00434 281 ASQTYMKGILGFT 293
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-173 7.22e-70

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 214.77  E-value: 7.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   1 DETARKHITAGAKKVVLTGPSK-DNTPMFVRGANFETYAGQD--IVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHAT 77
Cdd:PRK07403 104 KEGASKHIQAGAKKVLITAPGKgEDIGTYVVGVNHHEYDHEDhnIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSY 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  78 TATQKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKA 157
Cdd:PRK07403 184 TGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNEV 262

                        170
                 ....*....|....*.
gi 222522779 158 IKAASEGAMKGVLGYT 173
Cdd:PRK07403 263 LKDASEGPLKGILEYS 278
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 48-173 1.14e-68

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: 205.93  E-value: 1.14e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  48 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 127
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 222522779 128 AFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAASEGamKGVLGYT 173
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYT 124
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 2-170 4.82e-65

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 204.01  E-value: 4.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETYAGQD-IVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:PLN03096 165 EGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDpIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGD 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKA 160
Cdd:PLN03096 245 QRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRD 323

                        170
                 ....*....|
gi 222522779 161 ASEGAMKGVL 170
Cdd:PLN03096 324 AAEKELKGIL 333
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 4-173 4.11e-61

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 195.12  E-value: 4.11e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   4 ARKHITAGAKKVVLTGPSKDN-TPMFVRGANFETYAGQ--DIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAT 80
Cdd:PLN02237 182 AGKHIQAGAKKVIITAPAKGAdIPTYVVGVNEDDYDHEvaNIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGD 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  81 QKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAA-SYEEIKKAIK 159
Cdd:PLN02237 262 QRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFR 340

                        170
                 ....*....|....
gi 222522779 160 AASEGAMKGVLGYT 173
Cdd:PLN02237 341 KAADGPLKGILAVC 354
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
2-172 4.35e-56

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 178.97  E-value: 4.35e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSKD-NTPMFVRGANFETY--AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATT 78
Cdd:NF033735 100 EKLQPYFDQGVKKVVVSAPVKEeGVLNIVYGVNDHLYdpARHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDIT 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  79 ATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAI 158
Cdd:NF033735 180 NTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALF 258

                        170
                 ....*....|....
gi 222522779 159 KAASEGAMKGVLGY 172
Cdd:NF033735 259 KAAAEGPLKGILGY 272
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 6-173 5.49e-52

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 172.41  E-value: 5.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   6 KHITA-GAKKVVLTGPSKDNTPMFVRGANFETYAGQD-IVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKT 83
Cdd:PRK08289 245 QHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDkIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNL 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  84 VDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAAS- 162
Cdd:PRK08289 325 IDN-YHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSl 403

                        170
                 ....*....|.
gi 222522779 163 EGAMKGVLGYT 173
Cdd:PRK08289 404 HSPLQNQIDYT 414
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 6-172 1.84e-50

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 164.90  E-value: 1.84e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   6 KHITAGAKKVVLTGPSKDNTPM-FVRGANFETY--AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQK 82
Cdd:PRK08955 107 AYLDQGVKRVVVTAPVKEEGVLnIVMGVNDHLFdpAIHPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQT 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  83 TVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAAS 162
Cdd:PRK08955 187 ILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKEAA 265

                        170
                 ....*....|
gi 222522779 163 EGAMKGVLGY 172
Cdd:PRK08955 266 EGELKGILGY 275
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 2-173 1.66e-47

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 157.14  E-value: 1.66e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSK---DNTpmFVRGANFETYAGQD-IVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHAT 77
Cdd:PRK13535 106 EDGEAHIAAGAKKVLFSHPGSndlDAT--VVYGVNHDQLRAEHrIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  78 TATQKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKA 157
Cdd:PRK13535 184 MNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQL 262

                        170
                 ....*....|....*.
gi 222522779 158 IKAASEGAMKGVLGYT 173
Cdd:PRK13535 263 LQKAAQGAFHGIVDYT 278
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 48-173 2.56e-40

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: 133.69  E-value: 2.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  48 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 127
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 222522779 128 AFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAASEGAMKGVLGYT 173
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYT 125
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 48-173 3.72e-39

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: 130.72  E-value: 3.72e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  48 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWrgGRGAAQNIIPSSTGAAKAVGKVLPELN--GKLT 125
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 222522779 126 GMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAASEGAMKGVLGYT 173
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGL 126
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 7-173 9.86e-23

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 92.25  E-value: 9.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779   7 HITAGAKKVVLTGPSKDnTPMFVRGANFETY-AGQDIVSNASCTTNCLAPLAKVINDNFGIVEGLMTTVHATTAtQKTVD 85
Cdd:PTZ00353 112 HVTGGAKGVFVAGQSAD-APTVMAGSNDERLsASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHGMQP-QEPIA 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  86 GPSH--KDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAASE 163
Cdd:PTZ00353 190 ARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAAS 269

                        170
                 ....*....|
gi 222522779 164 GAMKGVLGYT 173
Cdd:PTZ00353 270 DRLNGVLCIS 279
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 2-47 9.53e-18

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: 75.51  E-value: 9.53e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 222522779   2 ETARKHITAGAKKVVLTGPSKDNTPMFVRGANFETY-AGQDIVSNAS 47
Cdd:cd05214  102 EKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYdADDKIISNAS 148
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 1-52 1.48e-06

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: 44.65  E-value: 1.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222522779   1 DETARKHITAGAKKVVLTGPSKDNTPMFVRG-ANFETYAGQDIVSNASCTTNC 52
Cdd:cd05192   47 DDNAEKHIKAGGKKAVITAPEKGDIPTIVVVlNELAKSAGATVVSNANETSYS 99
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 47-162 7.76e-04

C-terminal catalytic domain of type II 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 type II NADP+ utilizing GAPDHs, mainly from archaea.


Pssm-ID: 467677  Cd Length: 162  Bit Score: 37.95  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  47 SCTTNCLAPLAKVINDNFGIVEGlmttvhATTATQKTVDgPSHKDwrggRGAAQNIIPS---STGAAKAVGKVLPELNgk 123
Cdd:cd18127    1 SCNTTGLSRVLKALDRAFGLKRV------RATIVRRAAD-PGKHK----KGVINAIVPEpkdPSHHAPDVKTVFPDLD-- 67

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 222522779 124 LTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAAS 162
Cdd:cd18127   68 ITTSAVKVPTTLMHLHTINVELKRKVSREEVLEALASNP 106
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
28-162 1.46e-03

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 37.89  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222522779  28 FVRGANFETYAGQDIVSNASCTTNCLAPLAKVINDNFGIVEglmttVHATTATQKTVDGPSHkdwrggRGAAQNIIPSST 107
Cdd:PRK04207 120 FNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKK-----VRATLVRRAADPKEVK------RGPINAIVPDPV 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222522779 108 GA----AKAVGKVLPELNgkLTGMAFRVPTPNVSVVDLTVRLEKAASYEEIKKAIKAAS 162
Cdd:PRK04207 189 TVpshhGPDVKTVLPDLD--ITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEALENTP 245
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 2-47 1.63e-03

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: 37.25  E-value: 1.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 222522779   2 ETARKHITAGAKKVVLTGPSK---DNTpmFVRGANFETYAGQD-IVSNAS 47
Cdd:cd17892  105 EDAERHLAAGAKKVLFSHPASndvDAT--IVYGINQDLLRAEHrIVSNAS 152
 
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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