Q9KUS1 (PDXA_VIBCH) 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:	VC_0444

Organism

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae › Vibrio cholerae O1 › Vibrio cholerae O1 biovar El Tor

Protein attributes

Sequence length	330 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-Rule MF_00536
Catalytic activity	4-phosphonooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH. HAMAP-Rule 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-Rule MF_00536
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is located at the dimer interface By similarity. HAMAP-Rule 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 Reference proteome
Gene Ontology (GO)
Biological_process	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic process Inferred from sequence or structural similarity Ref.1. Source: TIGR
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4-hydroxythreonine-4-phosphate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP NAD binding Inferred from electronic annotation. Source: InterPro catalytic activity Inferred from sequence or structural similarity Ref.1. Source: TIGR cobalt ion binding Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 330	330	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_0000188833
Sites
	Metal binding	165	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	210	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	266	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	274	1	Substrate By similarity
	Binding site	283	1	Substrate By similarity
	Binding site	292	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KUS1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: EDA785D5D5513995	FASTA	330	35,605
	10 20 30 40 50 60 MSSKRIIVTA GEPAGIGPDL VLALSAQDWP HQLVVCADKA LLAQRATQLG IQVKLLDYQR 70 80 90 100 110 120 DNPVQAQQAG TLLVEHIPLA EPVVAGQLNP ANGHYVLKTL ERAAKGCMNG EFDAIVTGPV 130 140 150 160 170 180 HKGVINRAGV AFSGHTEFFA EQSKTPLVVM MLATEGLRTA LVTTHLPLAE VPQAITCERL 190 200 210 220 230 240 EQIVHILHKD LVEKFAIAEP KIYVCGLNPH AGEDGVLGMD EIETITPTLQ RLREQYGMQL 250 260 270 280 290 300 VGPLPADTIF SEKYLQQADA VLGMYHDQVL PVLKYKGFGR SVNITLGLPF IRTSVDHGTA 310 320 330 LDLAGTGQAD AGSFWTALAY AIELVDKKAQ

References

[1]

"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE003852 Genomic DNA. Translation: AAF93617.1.
PIR	C82323.
RefSeq	NP_230098.1. NC_002505.1.
3D structure databases
ProteinModelPortal	Q9KUS1.
SMR	Q9KUS1. Positions 1-325.
ModBase	Search...
Protein-protein interaction databases
STRING	243277.VC0444.
Protocols and materials databases
DNASU	2615776.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF93617; AAF93617; VC_0444.
GeneID	2615776.
KEGG	vch:VC0444.
PATRIC	20079967. VBIVibCho83274_0418.
Phylogenomic databases
eggNOG	COG1995.
KO	K00097.
OMA	AYVAMYH.
ProtClustDB	PRK00232.
Enzyme and pathway databases
UniPathway	UPA00244; UER00312.
Family and domain databases
Gene3D	3.40.718.10. 1 hit.
HAMAP	MF_00536. PdxA.
InterPro	IPR024084. IsoPropMal-DH-like_dom. IPR005255. PyrdxlP_synth_PdxA. [Graphical view]
Pfam	PF04166. PdxA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00557. pdxA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXA_VIBCH

Accession

Primary (citable) accession number: Q9KUS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 31, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program