EC Tree |
1. Oxidoreductases |
1.2 Acting on the aldehyde or oxo group of donors |
1.2.1 With NAD+ or NADP+ as acceptor |
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3IDS;
3DMT;
1QXS;
1ML3;
1K3T;
2PKR;
2PKQ;
1RM5;
1RM4;
1RM3;
1NBO;
1JN0;
2HKI;
1IHY;
1IHX;
1SZJ;
1CRW;
1I33;
1I32;
1GYQ;
1GYP;
1A7K;
4GPD;
1GPD;
2X0N;
1CF2;
1B7G;
1HDG;
1CER;
4DBV;
3DBV;
3CMC;
2GD1;
2DBV;
1GD1;
1DBV;
2CZC;
4WNC;
4WNI;
1ZNQ;
1U8F;
3GPD;
1GAE;
1GAD;
1DC6;
1DC5;
1DC4;
1DC3;
5ZA0;
1S7C;
6OK4;
6FZH;
5TSO;
5DDI;
4Z0H;
4O63;
4O59;
4K9D;
4IQ8;
3VAZ;
3V1Y;
3RVD;
3QV1;
3PYM;
3PFW;
3LVF;
3LC7;
3LC2;
3LC1;
3L6O;
3K73;
3K2B;
3HJA;
3H9E;
3E6A;
3E5R;
2YYY;
2XF8;
2X5J;
2I5P;
2EP7;
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UniProtKB Enzyme Link: | UniProtKB 1.2.1.12 |
BRENDA Enzyme Link: | BRENDA 1.2.1.12 |
KEGG Enzyme Link: | KEGG1.2.1.12 |
BioCyc Enzyme Link: | BioCyc 1.2.1.12 |
ExPASy Enzyme Link: | ExPASy1.2.1.12 |
EC2PDB Enzyme Link: | EC2PDB 1.2.1.12 |
ExplorEnz Enzyme Link: | ExplorEnz 1.2.1.12 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.2.1.12 |
IntEnz Enzyme Link: | IntEnz 1.2.1.12 |
MEDLINE Enzyme Link: | MEDLINE 1.2.1.12 |
RHEA:10300 | D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-phospho-D-glyceroyl phosphate + H(+) + NADH |
RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[n+;H0:4]1:[cH;+0:5]:[cH;+0:6]:[cH;+0:7]:[c;H0;+0:8](-[*:9]):[cH;+0:10]:1.[*:11]=[CH;+0:12]-[*:13]>>[*:3]-[N;H0;+0:4]1-[CH;+0:5]=[CH;+0:6]-[CH2;+0:7]-[C;H0;+0:8](-[*:9])=[CH;+0:10]-1.[*:11]=[C;H0;+0:12](-[*:13])-[O;H0;+0:2]-[*:1] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803. | Valverde F, Losada M, Serrano A | 1997 Jul | 9226260 |
Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. | Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, Aymerich S | 2000 May 12 | 10799476 |