Reviewed, UniProtKB/Swiss-Prot A0LIN6 (PDXA_SYNFM)

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.
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 – 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)
	A0LIN6-1 [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." 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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000478 Genomic DNA. Translation: ABK17288.1.
RefSeq	YP_845723.1.
3D structure databases
ModBase	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.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A0LIN6. MMLAGPS.
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_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:	June 16, 2009
This is version 19 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)