A7GFE5 (PDXA_CLOBL) 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:	CLI_2255

Organism

Clostridium botulinum (strain Langeland / NCTC 10281 / Type F) [Complete proteome] [HAMAP]

Taxonomic identifier

441772 [NCBI]

Taxonomic lineage

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

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_1000051499
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)
	A7GFE5 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: D48D3A43F3A457F6	FASTA	334	36,259
	10 20 30 40 50 60 MINNKPIIGI PIGDPAGVGP EIVVKSLTEA EVYEKCNPIL IGDAKVIKQA MGFCNVNLNI 70 80 90 100 110 120 NSIKKADEGK 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 AIVLAAKYSP KFKK

References

[1]	Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Langeland / NCTC 10281 / Type F.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000728 Genomic DNA. Translation: ABS39431.1.
RefSeq	YP_001391505.1. NC_009699.1.
3D structure databases
ProteinModelPortal	A7GFE5.
ModBase	Search...
Protein-protein interaction databases
STRING	441772.CLI_2255.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABS39431; ABS39431; CLI_2255.
GeneID	5402419.
KEGG	cbf:CLI_2255.
PATRIC	19427449. VBICloBot15611_2166.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221593.
KO	K00097.
OMA	EISVATM.
ProtClustDB	PRK03743.
Enzyme and pathway databases
BioCyc	CBOT441772:GJIE-2227-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_CLOBL

Accession

Primary (citable) accession number: A7GFE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program