Entry
Name
4-phosphoerythronate dehydrogenase;
PdxB;
PdxB 4PE dehydrogenase;
4-O-phosphoerythronate dehydrogenase;
4PE dehydrogenase;
erythronate-4-phosphate dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
4-phospho-D-erythronate:NAD+ 2-oxidoreductase
Reaction(IUBMB)
4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+ [RN:
R04210 ]
Reaction(KEGG)
Substrate
Product
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate [CPD:
C06054 ];
NADH [CPD:
C00004 ];
H+ [CPD:
C00080 ]
Comment
This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC
1.1.1.399 , 2-oxoglutarate reductase.
History
EC 1.1.1.290 created 2006, modified 2016
Pathway
Orthology
K03473 erythronate-4-phosphate dehydrogenase
Genes
ECOO : ECRM13514_3079(pdxB)
ECOH : ECRM13516_3022(pdxB)
ECW : EcE24377A_2614(pdxB)
EDJ : ECDH1ME8569_2258(pdxB)
ECOI : ECOPMV1_02479(pdxB)
REE : electrica_01430(pdxB)
RTG : NCTC13098_01933(pdxB)
CLAP : NCTC11466_01265(pdxB)
KIE : NCTC12125_00351(pdxB_1)
BAGE : BADSM9389_12260(pdxB)
AHN : NCTC12129_01487(pdxB)
METY : MRY16398_15800(pdxB)
PSHI : SAMEA2665130_0931(pdxB)
YPG : YpAngola_A0364(pdxB)
YPI : YpsIP31758_1418(pdxB)
SFJ : SAMEA4384070_3461(pdxB)
SOF : NCTC11214_03334(pdxB_2)
PAQU : DMB82_0007285(pdxB)
DIC : Dpoa569_001113(pdxB)
TPTY : NCTC11468_02532(pdxB_2)
PHEI : NCTC12003_01530(pdxB)
PRJ : NCTC6933_02367(pdxB)
LRI : NCTC12151_02328(pdxB)
VAU : VANGNB10_cI1916c(pdxB)
VPL : SA104470976_00708(pdxB)
PAEB : NCGM1900_5199(pdxB)
PVD : CFBP1590__1886(pdxB)
PPRC : PFLCHA0_c19870(pdxB)
PMUD : NCTC8068_01663(pdxB)
PFW : PF1751_v1c15320(pdxB)
PPUU : PputUW4_03530(pdxB)
PTRT : HU722_0008720(pdxB)
PTW : TUM18999_22210(pdxB)
PTAE : NCTC10697_01627(pdxB)
MSHE : MAALD49_17080(pdxB)
PSYC : DABAL43B_0350(pdxB)
ACUM : C9E88_016305 C9E88_17515
MCAT : MC25239_00426(pdxB)
MCUN : NCTC10297_00922(pdxB)
SCAA : TUM17387_16830(pdxB)
SALH : HMF8227_01955(pdxB)
CBS : COXBURSA331_A2011(pdxB)
LLG : 44548918_00815(pdxB)
LJR : NCTC11533_00950(pdxB)
LCJ : NCTC11976_01656(pdxB)
LWA : SAMEA4504053_1250(pdxB)
LSS : NCTC12082_00964(pdxB)
LADL : NCTC12735_01469(pdxB)
LANT : TUM19329_22870(pdxB)
TSE : THMIRHAS_20340(pdxB)
TZO : THMIRHAT_06200(pdxB)
HAXI : HAALTHF_47090n(pdxB)
AEL : NCTC12917_02512(pdxB)
PLG : NCTC10937_03640(pdxB)
BTHO : Btheta7330_04939(pdxB)
BCEL : BcellWH2_02474(pdxB)
BFC : BacF7301_06210(pdxB)
PCRE : NCTC12858_00048(pdxB)
PCAG : NCTC12856_01905(pdxB)
PSOE : CE91St14_15450(pdxB)
COPR : Cop2CBH44_24100(pdxB)
CFAS : Cfast33896_16850(pdxB)
ACOU : A5CBH24_07680(pdxB)
ADA : A5CPEGH6_08170(pdxB)
» show all
Taxonomy
Reference
Authors
Lam HM, Winkler ME.
Title
Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12.
Journal
Reference
Authors
Pease AJ, Roa BR, Luo W, Winkler ME
Title
Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12.
Journal
Sequence
Reference
Authors
Zhao G, Winkler ME
Title
A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria.
Journal
Reference
Authors
Grant GA.
Title
A new family of 2-hydroxyacid dehydrogenases.
Journal
Reference
Authors
Schoenlein PV, Roa BB, Winkler ME
Title
Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12.
Journal
Sequence
Reference
Authors
Rudolph J, Kim J, Copley SD
Title
Multiple turnovers of the nicotino-enzyme PdxB require alpha-keto acids as cosubstrates.
Journal
Other DBs
ExPASy - ENZYME nomenclature database: 1.1.1.290