Q65I57 (PANC_BACLD) 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:	BLi02377, BL02751

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	288 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 – 288	288	Pantothenate synthetase HAMAP MF_00158		PRO_0000128203
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

Sequences

	Sequence		Length	Mass (Da)
	Q65I57 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 4A9E5800166A9BDD	FASTA	288	32,464
	10 20 30 40 50 60 MIQIYTAKDI QNLTKNYRKE GKTIGFVPTM GFLHEGHMSL VEKARKDNDI VVMSIFVNPM 70 80 90 100 110 120 QFGPGEDYEA YPRDIERDRQ LAAGSGVDVL FTPEPEEMYG QEPTVTASVK KRTDVLCGRS 130 140 150 160 170 180 REGHFDGVAT VLTKLFNLTS PTRVYFGMKD AQQVAVVDGL INDFFMDIEL IPVETKREED 190 200 210 220 230 240 GLAKSSRNVN LRAEERQEAT ALYRALQRGA ELIRNGERDP EAVKREIRSI LEKTSGVIDY 250 260 270 280 ADIYSYPDLE IRDPLTGKVI IAVAVQFSKA RLIDNIIVDI PADQKEDL

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017333 Genomic DNA. Translation: AAU41257.1. CP000002 Genomic DNA. Translation: AAU23903.1.
RefSeq	YP_079541.1. NC_006270.3. YP_091950.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65I57.
SMR	Q65I57. Positions 1-278.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65I57.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000056922; EBBACP00000055453; EBBACG00000056913. EBBACT00000060176; EBBACP00000058609; EBBACG00000060167.
GeneID	3029463. 3100430.
GenomeReviews	Gene locus BLi02377 in contig AE017333_GR. Gene locus BL02751 in contig CP000002_GR.
KEGG	bld:BLi02377. bli:BL02751.
NMPDR	fig|279010.5.peg.227.
PATRIC	18950412. VBIBacLic203714_2408.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
GeneTree	EBGT00050000001451.
HOGENOM	HBG428839.
OMA	LNMPIQI.
PhylomeDB	Q65I57.
ProtClustDB	PRK00380.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI02377-MONOMER. BLIC279010:BL02751-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_BACLD

Accession

Primary (citable) accession number: Q65I57
Secondary accession number(s): Q62TK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program