A8A2I9 (PDXB_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Erythronate-4-phosphate dehydrogenase
EC=1.1.1.290

Gene names

Name:	pdxB
Ordered Locus Names:	EcHS_A2471

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate By similarity. HAMAP MF_01825
Catalytic activity	4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH. HAMAP MF_01825
Pathway	Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 2/5. HAMAP MF_01825
Subunit structure	Homodimer By similarity. HAMAP MF_01825
Subcellular location	Cytoplasm Potential HAMAP MF_01825.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. PdxB subfamily.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4-phosphoerythronate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 378	378	Erythronate-4-phosphate dehydrogenase HAMAP MF_01825		PRO_1000088418
Sites
	Active site	208	1	By similarity
	Active site	237	1	By similarity
	Active site	254	1	Proton donor By similarity
	Binding site	45	1	Substrate By similarity
	Binding site	66	1	Substrate By similarity
	Binding site	146	1	NAD By similarity
	Binding site	175	1	NAD; via carbonyl oxygen By similarity
	Binding site	232	1	NAD By similarity
	Binding site	257	1	NAD; via amide nitrogen By similarity
	Binding site	258	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8A2I9 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 665E4E6B6EBB03AF	FASTA	378	41,306
	10 20 30 40 50 60 MKILVDENMP YARDLFSRLG EVTAVPGRPI PVAQLADADA LMVRSVTKVN ESLLAGKPIK 70 80 90 100 110 120 FVGTATAGTD HVDEAWLKQA GIGFSAAPGC NAIAVVEYVF SSLLMLAERD GFSLHDRTVG 130 140 150 160 170 180 IVGVGNVGRR LQARLEALGI KTLLCDPPRA DRGDEGDFRS LDELVQHADI LTFHTPLFKD 190 200 210 220 230 240 GPYKTLHLAD EKLIRSLKPG AILINACRGA VVDNTALLTC LNEGQKLSVV LDVWEGEPEL 250 260 270 280 290 300 NVELLTKVDI GTPHIAGYTL EGKARGTTQV FEAYSKFIGH EQHVALDTLL PAPEFGRITL 310 320 330 340 350 360 HGPLDQPTLK RLVHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS SLYVICDDAS 370 AASLLCKLGF NAVHHPAR

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000802 Genomic DNA. Translation: ABV06743.1.
RefSeq	YP_001459126.1. NC_009800.1.
3D structure databases
ProteinModelPortal	A8A2I9.
SMR	A8A2I9. Positions 1-373.
ModBase	Search...
Protein-protein interaction databases
STRING	A8A2I9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000052646; EBESCP00000050631; EBESCG00000051694.
GeneID	5590970.
GenomeReviews	Gene locus EcHS_A2471 in contig CP000802_GR.
KEGG	ecx:EcHS_A2471.
PATRIC	18314922. VBIEscCol77814_2423.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0111.
GeneTree	EBGT00050000009079.
HOGENOM	HBG289972.
OMA	SAPGCNA.
ProtClustDB	PRK15438.
Family and domain databases
HAMAP	MF_01825. PdxB. [Tree]
InterPro	IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR020921. Erythronate-4-P_DHase. IPR024531. Erythronate-4-P_DHase_dimer. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
KO	K03473.
PANTHER	PTHR10996:SF4. Erythronate-4-P_DHase. 1 hit.
Pfam	PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. PF11890. DUF3410. 1 hit. [Graphical view]
PROSITE	PS00065. D_2_HYDROXYACID_DH_1. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. False negative. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXB_ECOHS

Accession

Primary (citable) accession number: A8A2I9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 23, 2007
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program