Reviewed, UniProtKB/Swiss-Prot A0RNS3 (PDXA_CAMFF)

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:	CFF8240_0681

Organism

Campylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP]

Taxonomic identifier

360106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	307 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 – 307	307	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP MF_00536		PRO_1000051492
Sites
	Metal binding	150	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	189	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	246	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	254	1	Substrate By similarity
	Binding site	263	1	Substrate By similarity
	Binding site	272	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0RNS3-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: A3439845911CFA96	FASTA	307	33,925
	10 20 30 40 50 60 MSLPKIAISV GDINGVGIEI ALKSHDEIKN ICSPIYFINN ELLNSAANIL KFTVPNDFEI 70 80 90 100 110 120 FECGSSFNIK PGRVSKKSGK FSFVSFENAI LYTQNKRAQA LVTMPINKES WKKAGVPYVG 130 140 150 160 170 180 HTDALGKYFG KNAIMMLGCE ELFVALYTDH LALKDVSAKI KAKNLALFLV DFYNSSKFEN 190 200 210 220 230 240 IGVLGFNPHA SDNETIGGKE EKEIIKAIKS ANNRLKKEVF TGPLVPDAAF TKSSLKRCNR 250 260 270 280 290 300 LVSMYHDVGL APLKALYFDK SINVSLNLPI VRTSVDHGTA FDIAYKGKAE TKSYIEAIKF AIKLCDY

References

[1]	"Sequence of Campylobacter fetus subsp. fetus 82-40." Fouts D.E., Nelson K.E. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000487 Genomic DNA. Translation: ABK83061.1.
RefSeq	YP_891856.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4538213.
GenomeReviews	Gene locus CFF8240_0681 in contig CP000487_GR.
KEGG	cff:CFF8240_0681.
NMPDR	fig|360106.5.peg.644.
TIGR	CFF8240_0681.
Phylogenomic databases
OMA	A0RNS3. DKSINVS.
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_CAMFF

Accession

Primary (citable) accession number: A0RNS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 9, 2007
Last modified:	June 16, 2009
This is version 19 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)