Q3V7K1 (PDXJ_SALPA) 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:	SPA0287

Organism

Salmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]

Taxonomic identifier

295319 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella paratyphi A

Protein attributes

Sequence length	243 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.
Subcellular location	Cytoplasm By similarity.
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 – 243	243	Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279		PRO_0000231844
Regions
	Region	11 – 12	2	1-deoxy-D-xylulose 5-phosphate binding By similarity
	Region	215 – 216	2	3-amino-2-oxopropyl phosphate binding By similarity
Sites
	Active site	45	1	Proton acceptor By similarity
	Active site	72	1	Proton acceptor By similarity
	Active site	193	1	Proton donor By similarity
	Binding site	9	1	3-amino-2-oxopropyl phosphate By similarity
	Binding site	20	1	3-amino-2-oxopropyl phosphate By similarity
	Binding site	47	1	1-deoxy-D-xylulose 5-phosphate By similarity
	Binding site	52	1	1-deoxy-D-xylulose 5-phosphate By similarity
	Binding site	102	1	1-deoxy-D-xylulose 5-phosphate By similarity
	Binding site	194	1	3-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
	Site	153	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3V7K1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 2AF9CD16A8114664	FASTA	243	26,313
	10 20 30 40 50 60 MAELLLGVNI DHIATLRNAR GTDYPDPVQA AFIAEQAGAD GITVHLREDR RHITDRDVRI 70 80 90 100 110 120 LRQTLHTRMN LEMAVTEEML AIAVETRPHF CCLVPEKRQE VTTEGGLDVA GQRDKMRDAC 130 140 150 160 170 180 ARLAAAGIQV SLFIDADEAQ INAAAEVGAP FIEIHTGCYA NAETDAEQAK ELARIASAAT 190 200 210 220 230 240 LAARLGLKVN AGHGLTYHNV KAIAALPEMH ELNIGHAIIG RAVMTGLKEA VAEMKRLMLE ARG

References

[1]

"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid." McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K. Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000026 Genomic DNA. Translation: AAV76309.1.
RefSeq	YP_149621.1. NC_006511.1.
3D structure databases
ProteinModelPortal	Q3V7K1.
SMR	Q3V7K1. Positions 2-243.
ModBase	Search...
Protein-protein interaction databases
STRING	295319.SPA0287.
Proteomic databases
PRIDE	Q3V7K1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV76309; AAV76309; SPA0287.
GeneID	3178757.
KEGG	spt:SPA0287.
PATRIC	32349686. VBISalEnt134188_0301.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000258095.
KO	K03474.
OMA	LHYHNVK.
ProtClustDB	PRK05265.
Enzyme and pathway databases
BioCyc	SENT295319:GJBZ-286-MONOMER.
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_SALPA

Accession

Primary (citable) accession number: Q3V7K1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	October 11, 2005
Last modified:	May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program