Q2N8X0 (PDXA_ERYLH) 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:	ELI_08895

Organism

Erythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]

Taxonomic identifier

314225 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Erythrobacteraceae › Erythrobacter › Erythrobacter litoralis

Protein attributes

Sequence length	336 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 – 336	336	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000051500
Sites
	Metal binding	171	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	216	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	271	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	140	1	Substrate By similarity
	Binding site	279	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	297	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2N8X0 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: 213B605C1BF17B80	FASTA	336	34,465
	10 20 30 40 50 60 MGEPQRPLAV SLGDPAGIGP EIIVHAWRMR DSANLAPFAV AGGANVLRSA TEALGVPCPI 70 80 90 100 110 120 QEIDDIAEAN SAFLEALPVI KGLDGAYLPG APDPIGAKLA LKSLEMATRL ATAGHASGVV 130 140 150 160 170 180 TAPIAKGLLE QVGFTHPGQT EFLAAACGLP EDASVMMLAG PSLRAVPLTV HCPLAEVPGL 190 200 210 220 230 240 LSIGLIVERG RIVASALQRD FGIERPRLAV TGLNPHAGED GKFGNEEQDV IAPAIAELLA 250 260 270 280 290 300 DGITATGPHP ADALFSPHSR AGFDAALCMY HDQALIPVKA LDFDQGVNVT LGLPIVRTSP 310 320 330 DHGTAFDIAG RGTAHPGAMV FALLMAGECA ARRADA

References

[1]	"Complete genome sequence of Erythrobacter litoralis HTCC2594." Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C. J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HTCC2594.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000157 Genomic DNA. Translation: ABC63871.1.
RefSeq	YP_458668.1. NC_007722.1.
3D structure databases
ProteinModelPortal	Q2N8X0.
ModBase	Search...
Protein-protein interaction databases
STRING	314225.ELI_08895.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABC63871; ABC63871; ELI_08895.
GeneID	3870181.
KEGG	eli:ELI_08895.
PATRIC	21860684. VBIEryLit102657_1765.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221592.
KO	K00097.
OMA	CAVAMYH.
Enzyme and pathway databases
BioCyc	ELIT314225:GHLE-1823-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_ERYLH

Accession

Primary (citable) accession number: Q2N8X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 7, 2006
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program