Reviewed, UniProtKB/Swiss-Prot A7ZW04 (PDXA_ECOHS)

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:	EcHS_A0058

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	4-(phosphonooxy)-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH. HAMAP 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 MF_00536
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is located at the dimer interface By similarity.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 or NADH binding Inferred from electronic annotation. Source: InterPro cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 MF_00536		PRO_1000061031
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)
	A7ZW04-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: F732A738D82FE1EC	FASTA	329	35,209
	10 20 30 40 50 60 MVKTQRVVIT PGEPAGIGPD LVVQLAQREW PVELVVCADA 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]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000802 Genomic DNA. Translation: ABV04458.1.
RefSeq	YP_001456841.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5592043.
GenomeReviews	Gene locus EcHS_A0058 in contig CP000802_GR.
KEGG	ecx:EcHS_A0058.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A7ZW04. TTKRIAI.
Family and domain databases
HAMAP	MF_00536. [Tree]
InterPro	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_ECOHS

Accession

Primary (citable) accession number: A7ZW04

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	June 16, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)