Q5P7J0 (PDXA_AROAE) 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:	AZOSEA05990
ORF Names:	ebA1139

Organism

Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]

Taxonomic identifier

76114 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum › Aromatoleum aromaticum

Protein attributes

Sequence length	326 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 – 326	326	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000051490
Sites
	Metal binding	160	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	205	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	260	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	268	1	Substrate By similarity
	Binding site	277	1	Substrate By similarity
	Binding site	286	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P7J0 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 41823413D100D43A	FASTA	326	33,572
	10 20 30 40 50 60 MASLPILAIT SGEPAGIGPE LCAQLSRRDW PLRPVVLGDF ELIRARAAGA AVVRAYMPDA 70 80 90 100 110 120 PAAAGVLDVL HVPLNVAARP GRLDPANAGY VLALLDRAVH GCRSGEFGAI VTAPVHKGVI 130 140 150 160 170 180 NDAGVAFSGH TEYLAEHTGT PRVVMMLVGG GLRVALATTH LPLAAVPGAI TPALLDETLR 190 200 210 220 230 240 ILHADLAGRF GLAAPRILVA GLNPHAGEGG HMGREEIDVI APVLERLRGE GMRLVGPLPA 250 260 270 280 290 300 DTLFVPHTLG QGDAVLAMYH DQGLPVLKHA SFGGGVNVTL GLPIIRTSVD HGTALDLAGT 310 320 GRADPGSLFA AVELATAMVC NRDVAR

References

[1]

"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1." Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R. Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: EbN1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR555306 Genomic DNA. Translation: CAI06721.1.
RefSeq	YP_157622.1. NC_006513.1.
3D structure databases
HSSP	HSSP built from PDB template 1YXO based on UniProtKB Q9I5U4.
ProteinModelPortal	Q5P7J0.
SMR	Q5P7J0. Positions 7-322.
ModBase	Search...
Protein-protein interaction databases
STRING	76114.ebA1139.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAI06721; CAI06721; ebA1139.
GeneID	3181388.
KEGG	eba:ebA1139.
PATRIC	20967277. VBIAroAro98752_0605.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221592.
KO	K00097.
OMA	RITHAAM.
ProtClustDB	PRK00232.
Enzyme and pathway databases
BioCyc	AARO76114:GJTA-612-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_AROAE

Accession

Primary (citable) accession number: Q5P7J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program