C3KYY3 (PDXA_CLOB6) 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:	CLJ_B2416

Organism

Clostridium botulinum (strain 657 / Type Ba4) [Complete proteome] [HAMAP]

Taxonomic identifier

515621 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium botulinum › Clostridium botulinum B

Protein attributes

Sequence length	334 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 – 334	334	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000211910
Sites
	Metal binding	171	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	215	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	141	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Binding site	278	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	C3KYY3 [UniParc]. Last modified June 16, 2009. Version 1. Checksum: 6E373CC452F25B1A	FASTA	334	36,314
	10 20 30 40 50 60 MINNKPIIGI PIGDPAGVGP EIVVKSLTQA EIYEKCNPIL IGDAKVIKQA MGFCNVNLNI 70 80 90 100 110 120 NSIKKVDEGK FTLGTIDLID LNNIDIDELK IGKVQGIAGK AAFEYIKKSV EMAKEGELDA 130 140 150 160 170 180 IATTPINKES LREGNVNYIG HTEILADLTD TEDPLTMFEV RGMRVFFLTR HVSLRKACDL 190 200 210 220 230 240 VTKERVLDYI IRCSEALEKL GVKDGKMAVA GLNPHSGEHG LFGDEEMKAV VPAIEEAQKM 250 260 270 280 290 300 GYKVEGPIGA DSVFHLALKG RYNSVLSLYH DQGHIATKTL DFERTIAVTN GMPILRTSVD 310 320 330 HGTAFDIAGT GQASSVSMVE AIILAAKYSP KFKK

References

[1]

"Genome sequence of Clostridium botulinum Ba4 strain 657." Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S. Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 657 / Type Ba4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001083 Genomic DNA. Translation: ACQ54394.1.
RefSeq	YP_002863183.1. NC_012658.1.
3D structure databases
ProteinModelPortal	C3KYY3.
ModBase	Search...
Protein-protein interaction databases
STRING	515621.CLJ_B2416.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACQ54394; ACQ54394; CLJ_B2416.
GeneID	7878960.
KEGG	cbi:CLJ_B2416.
PATRIC	19413183. VBICloBot19908_2621.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221593.
KO	K00097.
OMA	EISVATM.
ProtClustDB	PRK03743.
Enzyme and pathway databases
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_CLOB6

Accession

Primary (citable) accession number: C3KYY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program