B6HZ33 (PDXA_ECOSE) 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:	ECSE_0053

Organism

Escherichia coli (strain SE11) [Complete proteome] [HAMAP]

Taxonomic identifier

409438 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	329 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. HAMAP-Rule MF_00536
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00536.
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 – 329	329	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP-Rule MF_00536		PRO_1000128246
Sites
	Metal binding	166	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	211	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	266	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	274	1	Substrate By similarity
	Binding site	283	1	Substrate By similarity
	Binding site	292	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6HZ33 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: AC85A1E3B2935737	FASTA	329	35,239
	10 20 30 40 50 60 MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADT TLLTDRAAML GLPLTLRPYS 70 80 90 100 110 120 PNSPAQPQTT GTLTLLPVAL RESVTAGQLA IENGHYVVET LARACDGCLN GEFAALITGP 130 140 150 160 170 180 VHKGVINDAG IPFTGHTEFF EERSQAKKVV MMLATEELRV ALATTHLPLR DIADAITPAL 190 200 210 220 230 240 LHEVIAILHH DLRTKFGIAE PRILVCGLNP HAGEGGHMGT EEIDTIIPVL DELRAQGMKL 250 260 270 280 290 300 NGPLPADTLF QPKYLDNADA VLAMYHDQGL PVLKYQGFGR GVNITLGLPF IRTSVDHGTA 310 320 LELAGRGEAD VGSFITALNL AIKMIVNTQ

References

[1]

"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult." Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M. DNA Res. 15:375-386(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SE11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009240 Genomic DNA. Translation: BAG75577.1.
RefSeq	YP_002291328.1. NC_011415.1.
3D structure databases
ProteinModelPortal	B6HZ33.
SMR	B6HZ33. Positions 1-329.
ModBase	Search...
Protein-protein interaction databases
STRING	409438.ECSE_0053.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAG75577; BAG75577; ECSE_0053.
GeneID	6998424.
KEGG	ecy:ECSE_0053.
PATRIC	18418485. VBIEscCol83070_0170.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HOG000221592.
KO	K00097.
OMA	RITHAAM.
ProtClustDB	PRK00232.
Enzyme and pathway databases
BioCyc	ECOL409438:GHUU-53-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. PdxA. [Graphical view]
Pfam	PF04166. PdxA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00557. pdxA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXA_ECOSE

Accession

Primary (citable) accession number: B6HZ33

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	December 16, 2008
Last modified:	May 29, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program