Q1CR24 (PDXA_HELPH) 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:	HPAG1_1531

Organism

Helicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]

Taxonomic identifier

357544 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	307 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 – 307	307	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000051504
Sites
	Metal binding	156	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	195	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	251	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	126	1	Substrate By similarity
	Binding site	127	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity
	Binding site	268	1	Substrate By similarity
	Binding site	277	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1CR24 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: 8DCBBA3ABAE3B4A5	FASTA	307	33,780
	10 20 30 40 50 60 MAKKKIAISC GDIQGVGLEL ILKSHKEVSA FCEPLYLIDG ELLERANQLL HNAYETKTLN 70 80 90 100 110 120 TLAIHSPLPL LNSSTIGKVS AQSGAYSFES FKKACELADD KEVDGVCTLP INKLAWQQAQ 130 140 150 160 170 180 IPFVGHTDFL KQRYKDHQII MMLGCSKLFV GLFSDHVPLG AVSQLIQVKE LVKFLLAFQK 190 200 210 220 230 240 STQAKIVQVC GFNPHAGEEG LFGEEDEKIL KAIQKSNQTL GFECFLGPLP ADSAFAPNKR 250 260 270 280 290 300 KITPFYVSMS HDVGLAPLKA LYFDESINVS LNAPILRAST DHGTAFDIAY QNKANNKSYL NAIKYLA

References

[1]

"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression." Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HPAG1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000241 Genomic DNA. Translation: ABF85598.1.
RefSeq	YP_628272.1. NC_008086.1.
3D structure databases
ProteinModelPortal	Q1CR24.
ModBase	Search...
Protein-protein interaction databases
STRING	357544.HPAG1_1531.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABF85598; ABF85598; HPAG1_1531.
GeneID	4098403.
KEGG	hpa:HPAG1_1531.
PATRIC	20604535. VBIHelPyl56048_1586.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221591.
KO	K00097.
OMA	MFPGHTE.
ProtClustDB	PRK03946.
Enzyme and pathway databases
BioCyc	HPYL357544:GH1F-1571-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_HELPH

Accession

Primary (citable) accession number: Q1CR24

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 11, 2006
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program