A1JJF5 (PDXA_YERE8) 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:	YE0631

Organism

Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081) [Complete proteome] [HAMAP]

Taxonomic identifier

393305 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › Yersinia enterocolitica › Yersinia enterocolitica subsp. enterocolitica

Protein attributes

Sequence length	331 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 – 331	331	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000061035
Sites
	Metal binding	167	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	212	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	267	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	275	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1JJF5 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 52BF40C3951A4E59	FASTA	331	35,361
	10 20 30 40 50 60 MQNHNNRIVI TPGEPAGVGP DLVIALAQQD WPVELVVCAD PALLLTRASQ LNLPLQLREY 70 80 90 100 110 120 QQDKPALAQL AGTLTILPVK IAAEVIPGQL DVKNSHYVVE TLAKACDGAI SGEFAALVTG 130 140 150 160 170 180 PVQKSIINDA GIPFIGHTEF FADRSHCSRV VMMLATEELR VALATTHLPL LAVPGAITQT 190 200 210 220 230 240 SLHEVISILD NDLKTKFGIS QPQIYVCGLN PHAGEGGHMG HEEIETIIPA LATLRQQGIN 250 260 270 280 290 300 LIGPLPADTL FQPKYLQHAD AVLAMYHDQG LPVLKYQGFG RAVNITLGLP FIRTSVDHGT 310 320 330 ALELAATGTA DVGSFITALN LAIKMINNSN E

References

[1]

"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081." Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. , Quail M.A., Dougan G., Parkhill J., Prentice M.B. PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 8081.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286415 Genomic DNA. Translation: CAL10743.1.
RefSeq	YP_001004983.1. NC_008800.1.
3D structure databases
ProteinModelPortal	A1JJF5.
SMR	A1JJF5. Positions 7-329.
ModBase	Search...
Protein-protein interaction databases
STRING	393305.YE0631.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4712934.
KEGG	yen:YE0631.
PATRIC	18560672. VBIYerEnt11519_0724.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221592.
KO	K00097.
OMA	RITHAAM.
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_YERE8

Accession

Primary (citable) accession number: A1JJF5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	February 6, 2007
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