Q6AB12 (PDXA_PROAC) 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:	PPA0296

Organism

Propionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]

Taxonomic identifier

267747 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium › Propionibacterium acnes

Protein attributes

Sequence length	346 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 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	Metal-binding NAD NADP
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 metal 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 – 346	346	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000211915
Sites
	Metal binding	171	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	215	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	270	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Binding site	278	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6AB12 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 431C4C2534887BFD	FASTA	346	36,659
	10 20 30 40 50 60 MPKTPLLGIT EGDPAGIGPE ITVQAIHNMA DDRSFIPIVY GDPAIISRAC SVTGLSETVR 70 80 90 100 110 120 RVTSEEHIEP ESNVINVVDT GTVPHADSIE WGSVQELAGR AAIASIEAAT DAALSGKTDG 130 140 150 160 170 180 VVTSPINKEA IWKTGSEFLG HTEMLGSLCG TPDTDTMFVV SGLKIFFATR HMSLREAVDS 190 200 210 220 230 240 IRRDLIDHEI HKALRALKVF GCNSPKLAVA ALNPHAGEGG HFGTEEIEVL RPAVKSACAE 250 260 270 280 290 300 GHNVVGPVPA DSVFHKGVIR EYDGVLSLYH DQGHIASKTL DFDGTVSVTA GLPILRTSVD 310 320 330 340 HGTAFDIAGQ GAASPMTMQS ALHVASDFAR FVPVIREEYL PSTGRN

References

[1]

"The complete genome sequence of Propionibacterium acnes, a commensal of human skin." Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G. Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017283 Genomic DNA. Translation: AAT82054.1.
RefSeq	YP_055012.1. NC_006085.1.
3D structure databases
HSSP	HSSP built from PDB template 1PS6 based on UniProtKB P19624.
ProteinModelPortal	Q6AB12.
ModBase	Search...
Protein-protein interaction databases
STRING	267747.PPA0296.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT82054; AAT82054; PPA0296.
GeneID	2932160.
KEGG	pac:PPA0296.
PATRIC	23035247. VBIProAcn64440_0308.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221593.
KO	K00097.
OMA	EISVATM.
ProtClustDB	CLSK708077.
Enzyme and pathway databases
BioCyc	PACN267747:GHO9-348-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_PROAC

Accession

Primary (citable) accession number: Q6AB12

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	September 13, 2004
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program