Q5FNS3 (PDXA_GLUOX) 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:	GOX2240

Organism

Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP]

Taxonomic identifier

290633 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter › Gluconobacter oxydans

Protein attributes

Sequence length	334 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
Gene Ontology (GO)
Biological_process	pyridoxal phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP pyridoxine biosynthetic process Inferred from electronic annotation. Source: HAMAP
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 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 – 334	334	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000051502
Sites
	Metal binding	163	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	208	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	263	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	271	1	Substrate By similarity
	Binding site	280	1	Substrate By similarity
	Binding site	289	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5FNS3 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: B15C1C5680145CB4	FASTA	334	35,719
	10 20 30 40 50 60 MKRPPPLALT LGDPAGIGPQ LAAEAWRRLR HSGEGIFFWL GDPRLVERAV PVTCIATPEE 70 80 90 100 110 120 AAAVFADSLP VLPVPCEVEV IPGQPDSRNA AATITSIRQA VEYALAGRAG GVVTNPIAKH 130 140 150 160 170 180 VLAAAGFPYP GHTEFLAALC DMPGEEIMML ASPQLRVVPV TVHVSLRRAL ETLTTERIVQ 190 200 210 220 230 240 VAEIANAALR RDFGIMSPRL AIAGLNPHAG EHGMMGDEEI TIVQPAIDRL RAQGIDCRGP 250 260 270 280 290 300 MPPDTMFSDK ARPHYDVAIC MYHDQALIPL KTLDMEEGVN VTLGLPIIRT SPDHGTAFDI 310 320 330 AGPVTETCRA DVSSLLAAIW LAGEMSAYRE GRGS

References

[1]

"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans." Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U. Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 621H.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000009 Genomic DNA. Translation: AAW61974.1.
RefSeq	YP_192630.1. NC_006677.1.
3D structure databases
HSSP	HSSP built from PDB template 1YXO based on UniProtKB Q9I5U4.
ProteinModelPortal	Q5FNS3.
ModBase	Search...
Protein-protein interaction databases
STRING	290633.GOX2240.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAW61974; AAW61974; GOX2240.
GeneID	3249859.
KEGG	gox:GOX2240.
PATRIC	32612446. VBIGluOxy81109_2557.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221592.
KO	K00097.
OMA	CAVAMYH.
ProtClustDB	PRK05312.
Enzyme and pathway databases
BioCyc	GOXY290633:GHB3-2242-MONOMER.
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_GLUOX

Accession

Primary (citable) accession number: Q5FNS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 1, 2005
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program