Q8CUU4 (PDXA_OCEIH) 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:	OB1013

Organism

Oceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]

Taxonomic identifier

221109 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Oceanobacillus › Oceanobacillus iheyensis

Protein attributes

Sequence length	332 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
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 – 332	332	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_0000188813
Sites
	Metal binding	170	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	270	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	140	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	278	1	Substrate By similarity
	Binding site	287	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CUU4 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: ED62C9CA66FCB51A	FASTA	332	36,017
	10 20 30 40 50 60 MSKKPIIGIT MGDAAGVGPE IIIKSLRNRE LYEQAHPIVI GDTKMLERAA KILDVDVSFD 70 80 90 100 110 120 KKTKDEELMD TEFGKITCID LDILPEDLAY GEVSPVSGNA AFEYLRMAIE LANEGKIQAI 130 140 150 160 170 180 CTAPLNKEAL QKGGHMYPGH TEILAELTNT EEFSMMLSSP KLKVIHVTTH VGLIQAIQMI 190 200 210 220 230 240 KPERVHKVIQ LAHETLSNSG IKNPKIGVCG INPHAGENGL FGNGEEEEKI IPAIQQAVKE 250 260 270 280 290 300 GINVEGPLPA DTLFFRAQRG DFDIVVAMYH DQGHGPIKVL GLEAGVNITV GLPIIRTSVD 310 320 330 HGTAFDIAGK GIVDERSMLE ALHQAIELAP TK

References

[1]

"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments." Takami H., Takaki Y., Uchiyama I. Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000028 Genomic DNA. Translation: BAC12969.1.
RefSeq	NP_691934.1. NC_004193.1.
3D structure databases
ProteinModelPortal	Q8CUU4.
ModBase	Search...
Protein-protein interaction databases
STRING	221109.OB1013.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAC12969; BAC12969; BAC12969.
GeneID	1016871.
KEGG	oih:OB1013.
PATRIC	22793026. VBIOceIhe82024_1031.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221591.
KO	K00097.
OMA	MFPGHTE.
ProtClustDB	PRK00232.
Enzyme and pathway databases
BioCyc	OIHE221109:GI2A-1104-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_OCEIH

Accession

Primary (citable) accession number: Q8CUU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2003
Last sequence update:	March 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