A0LIN6 (PDXA_SYNFM) 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:	Sfum_1601

Organism

Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) [Complete proteome] [HAMAP]

Taxonomic identifier

335543 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Syntrophobacterales › Syntrophobacteraceae › Syntrophobacter

Protein attributes

Sequence length	345 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 – 345	345	4-hydroxythreonine-4-phosphate dehydrogenase HAMAP MF_00536		PRO_1000051520
Sites
	Metal binding	173	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	218	1	Divalent metal cation; shared with dimeric partner By similarity
	Metal binding	274	1	Divalent metal cation; shared with dimeric partner By similarity
	Binding site	143	1	Substrate By similarity
	Binding site	144	1	Substrate By similarity
	Binding site	282	1	Substrate By similarity
	Binding site	291	1	Substrate By similarity
	Binding site	300	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LIN6 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 030A0107EA02ED92	FASTA	345	36,533
	10 20 30 40 50 60 MSSSKPRIAL TMGDPCGVGP DVIAQALASP TLFECCTPIV VGDPSALQRS MALSGASKKV 70 80 90 100 110 120 LVLREPAELP DDPGSDRIPL IAPVELSGRD IEHGRPTAAT CGAVVRYIES AVAFALAGQV 130 140 150 160 170 180 RGVCTGPINK ARMHEHGFDF PGHTEFLQAL TGSRRVVMML AGPRLRVSLA TIHEALADVP 190 200 210 220 230 240 ALLNVEMLRE VIRITAEALI RDFGLQAPRL AVAGLNPHAG EEGRFGREEI EILRPAIESL 250 260 270 280 290 300 RPPGRCTVTG PYPADTLFQR AHAGEFDAVV AMYHDQGLVP IKLVHFYDAV NVSLGLPIVR 310 320 330 340 TSVDHGTAYD LAGTGRAHPG SLTAAVQLAA LMAHNRFAAV SPVVP

References

[1]

"Complete sequence of Syntrophobacter fumaroxidans MPOB." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Boone D.R. , Brockman F., Culley D., Ferry J., Gunsalus R., McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 10017 / MPOB.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000478 Genomic DNA. Translation: ABK17288.1.
RefSeq	YP_845723.1. NC_008554.1.
3D structure databases
ProteinModelPortal	A0LIN6.
ModBase	Search...
Protein-protein interaction databases
STRING	A0LIN6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4460101.
GenomeReviews	Gene locus Sfum_1601 in contig CP000478_GR.
KEGG	sfu:Sfum_1601.
NMPDR	fig|335543.6.peg.1649.
PATRIC	23848593. VBISynFum78438_1870.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1995.
HOGENOM	HBG451136.
OMA	RERIDIY.
PhylomeDB	A0LIN6.
Enzyme and pathway databases
BioCyc	SFUM335543:SFUM_1601-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_SYNFM

Accession

Primary (citable) accession number: A0LIN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 12, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program