Reviewed, UniProtKB/Swiss-Prot A1K9J6 (PDXA_AZOSB)

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:	azo2885

Organism

Azoarcus sp. (strain BH72) [Complete proteome] [HAMAP]

Taxonomic identifier

62928 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Azoarcus

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	4-(phosphonooxy)-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH. HAMAP 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 MF_00536
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is located at the dimer interface By similarity.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 or NADH binding Inferred from electronic annotation. Source: InterPro cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 330	330	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP MF_00536		PRO_1000051489
Sites
	Metal binding	163	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	208	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	263	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	134	1	Substrate By similarity
	Binding site	271	1	Substrate By similarity
	Binding site	280	1	Substrate By similarity
	Binding site	289	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1K9J6-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 6479DC89D6006E5C	FASTA	330	33,928
	10 20 30 40 50 60 MAALPVLAVT SGEPAGVGPE LCARLLARDW PARLVVLGDA DLIAARAAAV GSPIAVRHYS 70 80 90 100 110 120 RGQAQAAGVL EVLHIPLAEP SDAGRLAVGN ARYVLALLDR ALAGCVGGEF AGMVTAPVHK 130 140 150 160 170 180 GVICESGIAF SGHTEYLAEH TATPLVVMML VGGGMRVALA TTHLPLAAVS AAITRPVLEQ 190 200 210 220 230 240 TLRILHADLV QRFGIAAPRI LVAGLNPHAG EGGHMGREEI EVITPVLDRL RAEGLQLVGP 250 260 270 280 290 300 LPADTLFAPH TLAHGDAVLA MYHDQGLPVL KHASFGGGVN VTLGLPVIRT SVDHGTALDL 310 320 330 AGSGRADPGS LYAAVELAVS MAEARARQPR

References

[1]

"Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp. strain BH72." Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J., Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C., Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J., Weidner S. , Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A. Nat. Biotechnol. 24:1385-1391(2006) [PubMed: 17057704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM406670 Genomic DNA. Translation: CAL95501.1.
RefSeq	YP_934388.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4609107.
GenomeReviews	Gene locus azo2885 in contig AM406670_GR.
KEGG	azo:azo2885.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A1K9J6. HAGEDGC.
Family and domain databases
HAMAP	MF_00536. [Tree]
InterPro	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_AZOSB

Accession

Primary (citable) accession number: A1K9J6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)