Q0VQC3 (PDXB_ALCBS) 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:	ABO_1177

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	371 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.
Sequence caution	The sequence CAL16625.1 differs from that shown. Reason: Erroneous initiation.

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 – 371	371	Erythronate-4-phosphate dehydrogenase HAMAP MF_01825		PRO_0000297432
Sites
	Active site	208	1	By similarity
	Active site	237	1	By similarity
	Active site	254	1	Proton donor By similarity
	Binding site	44	1	Substrate By similarity
	Binding site	65	1	Substrate By similarity
	Binding site	145	1	NAD 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)
	Q0VQC3 [UniParc]. Last modified July 24, 2007. Version 2. Checksum: FDD804685E481E99	FASTA	371	39,938
	10 20 30 40 50 60 MHIIADANMP GLEPFEAFAT VERVDGRSLT REQLGDADVL LVRSVTRVDR ALLAGSQVKF 70 80 90 100 110 120 VGSATIGTDH VDLAYLSEAG IQFAHAPGCN ARAVAEYVLQ AVLLLCARQG REVQGARVAV 130 140 150 160 170 180 VGLGNVGRRV ADWLSALGME VRGCDPLLDA QGYAGPVALA PLDDLLDADI ITLHVPLTQS 190 200 210 220 230 240 GEHATGHLLD ASRLSRLGPG QMLINTCRGP VIDNLALSQQ LASGTGPMTV LDVWETEPQV 250 260 270 280 290 300 PATLYQQVVM GSPHIAGYSL EGKLKGTSML YDAVCQWSGQ GIASGTAMAD APPLNPAVNS 310 320 330 340 350 360 EADLLALLQV AYRLEDDHRR LGESLHDTDP SAAFDRLRKH YPVRHELHYW QYDGSVDDTW 370 RAIISRLFEP D

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK2 / ATCC 700651 / DSM 11573.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL16625.1. Different initiation.
RefSeq	YP_692897.1. NC_008260.1.
3D structure databases
ProteinModelPortal	Q0VQC3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VQC3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4212449.
GenomeReviews	Gene locus ABO_1177 in contig AM286690_GR.
KEGG	abo:ABO_1177.
NMPDR	fig|393595.12.peg.1189.
PATRIC	20840095. VBIAlcBor124741_1238.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0111.
HOGENOM	HBG289972.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1177-MONOMER.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXB_ALCBS

Accession

Primary (citable) accession number: Q0VQC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	July 24, 2007
Last modified:	January 25, 2012
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program