A8G9P1 (PDXA_SERP5) 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:	Spro_0725

Organism

Serratia proteamaculans (strain 568) [Complete proteome] [HAMAP]

Taxonomic identifier

399741 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia

Protein attributes

Sequence length	330 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 MF_00536
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. HAMAP MF_00536
Subcellular location	Cytoplasm By similarity HAMAP MF_00536.
Miscellaneous	The active site is located at the dimer interface By similarity. HAMAP 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	pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4-hydroxythreonine-4-phosphate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro metal 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 – 330	330	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP MF_00536		PRO_1000061033
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)
	A8G9P1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 031CDA1113DF029D	FASTA	330	35,205
	10 20 30 40 50 60 MHNNNRIVIT PGEPAGVGPD LVAALAQQDW PVELVVCADP ALLLERARQL DLPLQLRTYQ 70 80 90 100 110 120 PQQPAQPQRA GTLTVLPVAT AHPVVAGELN VGNSAYVVET LARACDGCLN GEFAALITGP 130 140 150 160 170 180 VNKGVINDAG VPFIGHTEFF ADRSGCDRVV MMLATEELRV ALATTHLPLL AVPGAITRQS 190 200 210 220 230 240 LHEVIRILDH DLKTKFGLAQ PQIYVCGLNP HAGEGGHMGR EEIDTIIPAL DELRAEGITL 250 260 270 280 290 300 IGPLPADTLF QPKYLQHADA VLAMYHDQGL PVLKYQGFGR AVNITLGLPF IRTSVDHGTA 310 320 330 LELAGTGTAD AGSFKTALNL AIKMIINCNE

References

[1]

"Complete sequence of chromosome of Serratia proteamaculans 568." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000826 Genomic DNA. Translation: ABV39831.1.
RefSeq	YP_001476959.1. NC_009832.1.
3D structure databases
ProteinModelPortal	A8G9P1.
SMR	A8G9P1. Positions 1-327.
ModBase	Search...
Protein-protein interaction databases
STRING	A8G9P1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5605069.
GenomeReviews	Gene locus Spro_0725 in contig CP000826_GR.
KEGG	spe:Spro_0725.
PATRIC	32414090. VBISerPro44537_0752.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HBG451136.
OMA	INLAGPY.
ProtClustDB	PRK00232.
Enzyme and pathway databases
BioCyc	SPRO399741:SPRO_0725-MONOMER.
Family and domain databases
HAMAP	MF_00536. PdxA. [Tree]
InterPro	IPR005255. PyrdxlP_synth_PdxA. [Graphical view]
KO	K00097.
Pfam	PF04166. PdxA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00557. PdxA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXA_SERP5

Accession

Primary (citable) accession number: A8G9P1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program