Reviewed, UniProtKB/Swiss-Prot Q8XCR0 (PDXB_ECO57)

Names and origin

Protein names

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

Gene names

Name:	pdxB
Ordered Locus Names:	Z3582, ECs3204

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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_0000075977
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)
	Q8XCR0-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 9F03F5E59931F4FF	FASTA	378	41,298
	10 20 30 40 50 60 MKILVDENMP YARDLFSRLG EVIAVPGRPI PVAQLADADA LMVRSVTKVN ESLLAGKPIK 70 80 90 100 110 120 FVGTATAGTD HVDEAWLKQA GIGFSAAPGC NAIAVVEYVF SSLLMLAERD GFSLHERTVG 130 140 150 160 170 180 IVGVGNVGRR LQARLEALGI KTLLCDPPRA DCGDEGDFRS LDELVQRADI 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]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG57449.1. BA000007 Genomic DNA. Translation: BAB36627.1.
PIR	D91029. E85873.
RefSeq	NP_288894.1. NP_311231.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	915698. 957490.
GenomeReviews	Gene locus Z3582 in contig AE005174_GR. Gene locus ECs3204 in contig BA000007_GR.
KEGG	ece:Z3582. ecs:ECs3204.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8XCR0.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3204-MON.
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_ECO57

Accession

Primary (citable) accession number: Q8XCR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 43 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)