Q8G2J0 (PANC_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pantothenate synthetase
Short name=PS
EC=6.3.2.1

Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme

Gene names

Name:	panC
Ordered Locus Names:	BR0329, BS1330_I0330

Organism

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

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	293 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP MF_00158
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP MF_00158
Subunit structure	Homodimer By similarity. HAMAP MF_00158
Subcellular location	Cytoplasm Potential HAMAP MF_00158.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158
Sequence similarities	Belongs to the pantothenate synthetase family.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantoate-beta-alanine ligase 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 – 293	293	Pantothenate synthetase HAMAP MF_00158		PRO_0000128211
Regions
	Nucleotide binding	30 – 37	8	ATP By similarity
	Nucleotide binding	147 – 150	4	ATP By similarity
	Nucleotide binding	184 – 187	4	ATP By similarity
Sites
	Active site	37	1	Proton donor By similarity
	Binding site	61	1	Beta-alanine By similarity
	Binding site	61	1	Pantoate By similarity
	Binding site	153	1	Pantoate By similarity
	Binding site	176	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G2J0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: A242EC983D00F6D1	FASTA	293	32,554
	10 20 30 40 50 60 MQIIHTIEEL RQALAPARQQ GKKIGFVPTM GYLHKGHLEL VRRARVENDV TLVSIFVNPL 70 80 90 100 110 120 QFGANEDLGR YPRDLERDAG LLHDAQVDYL FAPTVSDMYP RPMQTVVDVP PLGNQMEGEA 130 140 150 160 170 180 RPGHFAGVAT VVSKLFNIVG PDAAYFGEKD FQQLVIIRRM VDDMAIPVRI VGVETVREDD 190 200 210 220 230 240 GLACSSRNVY LTPEQRRAAI IVPQALDEAD RLYRSGMDDP DALEAAIRTF ISRQPLAVPE 250 260 270 280 290 VIAIRDPETL ERLPALQGRP ILVALFVRVG ATRLLDNRVI GHAAPQITQE RAA

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: 12271122] [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: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014291 Genomic DNA. Translation: AAN29278.1. CP002997 Genomic DNA. Translation: AEM17691.1.
RefSeq	NP_697363.1. NC_004310.3.
3D structure databases
ProteinModelPortal	Q8G2J0.
SMR	Q8G2J0. Positions 1-281.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1165990.
GenomeReviews	Gene locus BR0329 in contig AE014291_GR.
KEGG	bms:BR0329.
NMPDR	fig|204722.1.peg.320.
PATRIC	17788947. VBIBruSui107850_0342.
TIGR	BR0329.
Phylogenomic databases
HOGENOM	HBG428839.
OMA	LNMPIQI.
PhylomeDB	Q8G2J0.
ProtClustDB	PRK00380.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_0329-MONOMER.
Family and domain databases
HAMAP	MF_00158. PanC. [Tree]
InterPro	IPR004821. Cyt_trans-rel. IPR003721. Pantoate_ligase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01918.
PANTHER	PTHR21299:SF1. Pantoate_ligase. 1 hit.
Pfam	PF02569. Pantoate_ligase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00125. Cyt_tran_rel. 1 hit. TIGR00018. PanC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANC_BRUSU

Accession

Primary (citable) accession number: Q8G2J0
Secondary accession number(s): G0K685

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program