B2IDU5 (PDXA_BEII9) 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:	Bind_3318

Organism

Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712) [Complete proteome] [HAMAP]

Taxonomic identifier

395963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Beijerinckiaceae › Beijerinckia › Beijerinckia indica › Beijerinckia indica subsp. indica

Protein attributes

Sequence length	337 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 – 337	337	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000128236
Sites
	Metal binding	168	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	212	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	267	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	138	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	275	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Binding site	293	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2IDU5 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 3321DC56A477BFA8	FASTA	337	35,408
	10 20 30 40 50 60 MVMLDHPLAV TMGDPSGIGP EIIAKMYLRR PDKRNWIVVG DPLVMEHAIA NLGVAVQIRR 70 80 90 100 110 120 IATVEEAGCE DGVLNVLASS SLATLPAVGR VSAVSGQAAY DAIVTAIGLA RQGTIRGIVT 130 140 150 160 170 180 APIHKEALAA AGIHYPGHTE ILAEQGGAQH VAMMLANDEI RTVLVTIHCS LADAIRKADF 190 200 210 220 230 240 PAQMQAIRLA HEGARALGIV QPRIAVAGLN PHAGEGGLFG DEEIRIITPA IAAARAEGID 250 260 270 280 290 300 ATGPWPGDTV FMQARLGKFD VVVAQYHDQG LIPVKFMGLE KGVNITLGLP FVRTSPDHGT 310 320 330 AFDIAGRGIA DSSSLETAFD YATRLKVPTP FFSGAMS

References

[1]

"Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC 9039." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N. , Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9039 / DSM 1715 / NCIB 8712.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001016 Genomic DNA. Translation: ACB96877.1.
RefSeq	YP_001834366.1. NC_010581.1.
3D structure databases
ProteinModelPortal	B2IDU5.
ModBase	Search...
Protein-protein interaction databases
STRING	395963.Bind_3318.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACB96877; ACB96877; Bind_3318.
GeneID	6199731.
KEGG	bid:Bind_3318.
PATRIC	21089729. VBIBeiInd21058_3772.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221593.
KO	K00097.
OMA	ADTLFHF.
ProtClustDB	CLSK984533.
Enzyme and pathway databases
BioCyc	BIND395963:GJA7-3373-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_BEII9

Accession

Primary (citable) accession number: B2IDU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	June 10, 2008
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program