Reviewed, UniProtKB/Swiss-Prot Q8FFH2 (PDXB_ECOL6)

Names and origin

Protein names

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

Gene names

Name:	pdxB
Ordered Locus Names:	c2865

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Subcellular location	Cytoplasm Potential.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4-phosphoerythronate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD or NADH binding 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_0000075976
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)
	Q8FFH2-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 275E565614881154	FASTA	378	41,347
	10 20 30 40 50 60 MKILVDENMP YARDLFSRLG EVTAVPGRPI PVAQLADADA LMVRSVTKVN ESLLAGKPIK 70 80 90 100 110 120 FVGTATAGTD HVDEAWLKQA GIGFSAAPGC NAIAVVEYVF SSLLMLAERD GFSLHERTVG 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 NVELLKKVDI GTPHIAGYTL EGKARGTTQV FEAYSKFIGH EQHVALDTLL PAPEFGRITL 310 320 330 340 350 360 HGPLDQPTLK RLVHLVYDVR RDDAPLRKVA GIPGEFDKLR KNYLERREWS SLYVICDDAS 370 AASLLCKLGF NAVHHPAR

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014075 Genomic DNA. Translation: AAN81317.1.
RefSeq	NP_754749.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1038420.
GenomeReviews	Gene locus c2865 in contig AE014075_GR.
KEGG	ecc:c2865.
NMPDR	fig|199310.1.peg.2792.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8FFH2.
OMA	Q8FFH2. SAPGCNA.
Enzyme and pathway databases
BRENDA	1.1.1.290. 292881.
Family and domain databases
HAMAP	MF_01825. [Tree]
InterPro	IPR006139. D-isomer_2_OHA_DH. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 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_ECOL6

Accession

Primary (citable) accession number: Q8FFH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)