Q89ZK3 (PDXA_BACTN) 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:	BT_4374

Organism

Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]

Taxonomic identifier

226186 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Bacteroidetes/Chlorobi group › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides › Bacteroides thetaiotaomicron

Protein attributes

Sequence length	364 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 Reference 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 – 364	364	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000051491
Sites
	Metal binding	169	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	214	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	269	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	277	1	Substrate By similarity
	Binding site	286	1	Substrate By similarity
	Binding site	295	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q89ZK3 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: FD60351E6D30985A	FASTA	364	40,325
	10 20 30 40 50 60 MEENKIRIGI TQGDINGVGY EVILKTFSDP TMLELCTPII YGSPKVAAYH RKALDVQANF 70 80 90 100 110 120 SIVNTASEAG YNRLSVVNCT DDEVKVEFSK PDPEAGKAAL GALERAIEEY REGLIDVIVT 130 140 150 160 170 180 APINKHTIQS EEFSFPGHTE YIEERLGNGN KSLMILMKND FRVALVTTHI PVREIATTIT 190 200 210 220 230 240 KELIQEKLMI FHRCLKQDFG IGAPRIAVLS LNPHAGDGGL LGMEEQEIII PAMKEMEEKG 250 260 270 280 290 300 IICYGPYAAD GFMGSGNYTH FDGILAMYHD QGLAPFKALA MEDGVNYTAG LPVVRTSPAH 310 320 330 340 350 360 GTAYDIAGKG LASEDSFRQA IYVAIDVFRN RQREKAARVN PLRKQYYEKR DDSDKLKLDT VDED

References

[1]

"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015928 Genomic DNA. Translation: AAO79479.1.
RefSeq	NP_813285.1. NC_004663.1.
3D structure databases
HSSP	HSSP built from PDB template 1R8K based on UniProtKB P58717.
ProteinModelPortal	Q89ZK3.
ModBase	Search...
Protein-protein interaction databases
STRING	226186.BT_4374.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO79479; AAO79479; BT_4374.
GeneID	1071722.
KEGG	bth:BT_4374.
PATRIC	21063810. VBIBacThe70966_4451.
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221591.
KO	K00097.
OMA	QILLASH.
ProtClustDB	CLSK823916.
Enzyme and pathway databases
BioCyc	BTHE226186:GJXV-4454-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_BACTN

Accession

Primary (citable) accession number: Q89ZK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program