Q8FZT6 (PDXJ_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyridoxine 5'-phosphate synthase
Short name=PNP synthase
EC=2.6.99.2

Gene names

Name:	pdxJ
Ordered Locus Names:	BR1385, BS1330_I1379

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate By similarity. HAMAP-Rule MF_00279
Catalytic activity	1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O. HAMAP-Rule MF_00279
Pathway	Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. HAMAP-Rule MF_00279
Subunit structure	Homooctamer; tetramer of dimers By similarity. HAMAP-Rule MF_00279
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00279.
Sequence similarities	Belongs to the PNP synthase family.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	pyridoxine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	pyridoxine 5'-phosphate synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 246	246	Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279		PRO_0000190110
Regions
	Region	221 – 222	2	3-amino-2-oxopropyl phosphate binding By similarity
Sites
	Active site	44	1	Proton acceptor By similarity
	Active site	76	1	Proton acceptor By similarity
	Active site	198	1	Proton donor By similarity
	Binding site	8	1	3-amino-2-oxopropyl phosphate By similarity
	Binding site	19	1	3-amino-2-oxopropyl phosphate By similarity
	Binding site	46	1	1-deoxy-D-xylulose 5-phosphate By similarity
	Binding site	51	1	1-deoxy-D-xylulose 5-phosphate By similarity
	Binding site	106	1	1-deoxy-D-xylulose 5-phosphate By similarity
	Binding site	199	1	3-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
	Site	157	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FZT6 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 6E44F12BD0FC15CF	FASTA	246	26,447
	10 20 30 40 50 60 MPAKLSVNLN AIAMLRNRRD LPWPSVTGLG RAALAAGAAG LTVHPRPDQR HIRFSDLGDI 70 80 90 100 110 120 RALIDDEYPQ AEFNIEGFPS EAFLDLVEKH EPEQVTLVPD DPMQATSDHG WDFMSKADFL 130 140 150 160 170 180 APIVARLKGR GMRVSLFADP DSLGYERAKA IGADHVELYT GPYGATHDDP AAAARELDRL 190 200 210 220 230 240 EKAARAATAL GLAVNAGHDL TVDNLPALVK RIPQLAEVSI GHGLTADALM YGIPVTVSRY ITALAG

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN30298.1. CP002997 Genomic DNA. Translation: AEM18714.1.
RefSeq	NP_698383.1. NC_004310.3. YP_005616206.1. NC_017251.1.
3D structure databases
ProteinModelPortal	Q8FZT6.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BR1385.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN30298; AAN30298; BR1385. AEM18714; AEM18714; BS1330_I1379.
GeneID	1167067. 12138418.
KEGG	bms:BR1385. bsi:BS1330_I1379.
PATRIC	17791125. VBIBruSui107850_1409.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0854.
HOGENOM	HOG000258095.
KO	K03474.
OMA	LHYHNVK.
ProtClustDB	PRK05265.
Enzyme and pathway databases
UniPathway	UPA00244; UER00313.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00279. PdxJ.
InterPro	IPR013785. Aldolase_TIM. IPR004569. PyrdxlP_synth_PdxJ. [Graphical view]
Pfam	PF03740. PdxJ. 1 hit. [Graphical view]
SUPFAM	SSF63892. PyrdxlP_synth_PdxJ. 1 hit.
TIGRFAMs	TIGR00559. pdxJ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDXJ_BRUSU

Accession

Primary (citable) accession number: Q8FZT6
Secondary accession number(s): G0KB68

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program