P65681 (PDXA_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxythreonine-4-phosphate dehydrogenase
EC=1.1.1.262

Alternative name(s):
4-(phosphohydroxy)-L-threonine dehydrogenase

Gene names

Name:	pdxA
Ordered Locus Names:	BR0683, BS1330_I0679

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP) By similarity. HAMAP MF_00536
Catalytic activity	4-(phosphonooxy)-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH. HAMAP MF_00536
Cofactor	Binds 1 divalent metal cation per subunit. Can use ions such as zinc, magnesium or cobalt By similarity.
Pathway	Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 4/5. HAMAP MF_00536
Subunit structure	Homodimer By similarity. HAMAP MF_00536
Subcellular location	Cytoplasm By similarity HAMAP MF_00536.
Miscellaneous	The active site is located at the dimer interface By similarity. HAMAP MF_00536
Sequence similarities	Belongs to the pdxA family.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Ligand	Cobalt Magnesium Metal-binding NAD NADP Zinc
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-hydroxythreonine-4-phosphate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 343	343	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP MF_00536		PRO_0000188801
Sites
	Metal binding	176	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	221	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	276	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity
	Binding site	302	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P65681 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: FBF6CA0AB6D28617	FASTA	343	36,193
	10 20 30 40 50 60 MRAKPLPPLA VSIGDPSGIG ADVALAAWLK RCELSLPPFF LIADPKQLAA RARHLGLAVD 70 80 90 100 110 120 FAILSDPREA EAAFGERLPL LALKHSHTES PGKPLTENAA GVIEAIERAV ELTLKGEAAA 130 140 150 160 170 180 VVTCPIAKKP LYEAGFQHPG HTEFLAELAG HHLGKPVTPV MMLAGPQLRA VPVTIHIPLS 190 200 210 220 230 240 EVPARLTTTE IVAVSRITAN ELRERFGIAS PRLAISGLNP HAGEGGALGK EDDAIILPAI 250 260 270 280 290 300 EQLIREGIDA RGPLPADTMF HAPARATYDA AICMYHDQAL IPAKALAFDE TVNVTLGLPF 310 320 330 340 IRTSPDHGTA FDIAGKGIAR PDSLVAAMRL AQQLAENAAS RNA

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29612.1. CP002997 Genomic DNA. Translation: AEM18029.1.
RefSeq	NP_697697.1. NC_004310.3.
3D structure databases
ProteinModelPortal	P65681.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1166346.
GenomeReviews	Gene locus BR0683 in contig AE014291_GR.
KEGG	bms:BR0683.
PATRIC	17789657. VBIBruSui107850_0695.
TIGR	BR0683.
Phylogenomic databases
HOGENOM	HBG451136.
OMA	LETAYQM.
PhylomeDB	P65681.
ProtClustDB	PRK05312.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0683-MONOMER.
Family and domain databases
HAMAP	MF_00536. PdxA. [Tree]
InterPro	IPR005255. PyrdxlP_synth_PdxA. [Graphical view]
KO	K00097.
Pfam	PF04166. PdxA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00557. PdxA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXA_BRUSU

Accession

Primary (citable) accession number: P65681
Secondary accession number(s): G0K824, P58712

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program