Q63DJ2 (PANC_BACCZ) 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:	BCE33L1423

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	282 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 – 282	282	Pantothenate synthetase HAMAP MF_00158		PRO_0000305396
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)
	Q63DJ2 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 996C3A82645EDCDB	FASTA	282	32,010
	10 20 30 40 50 60 MKIVTTVQEM QHITKELRAS GKSIGFVPTM GYLHEGHATL LRKAREENEI VVLSVFVNPL 70 80 90 100 110 120 QFGPNEDLDR YPRDIDRDEN VAKENGVDYL FYPSVEEMYP AEQTTTVEVV KRTDVLCGKQ 130 140 150 160 170 180 RPGHFAGVAT VLMKLFNITL PTRAYFGMKD AQQVAVIEGF VADFNIPVTI VRVDIVREED 190 200 210 220 230 240 GLAKSSRNVY LSQEERKEAP HLYRSLCMAK ERIEAGERNA EIITTLVKEY IETYTKGTVD 250 260 270 280 YADLYAYPSL QVVDQIEGRI ILAIAVKFEN VRLIDNITLT VK

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU18827.1.
RefSeq	YP_083020.1. NC_006274.1.
3D structure databases
HSSP	HSSP built from PDB template 1IHO based on UniProtKB P31663.
ProteinModelPortal	Q63DJ2.
SMR	Q63DJ2. Positions 1-279.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63DJ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000041524; EBBACP00000040425; EBBACG00000041515.
GeneID	3024889.
GenomeReviews	Gene locus BCE33L1423 in contig CP000001_GR.
KEGG	bcz:BCZK1423.
PATRIC	18886312. VBIBacCer95304_1495.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
GeneTree	EBGT00050000001451.
HOGENOM	HBG428839.
OMA	EMDGLAM.
PhylomeDB	Q63DJ2.
ProtClustDB	PRK00380.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L1423-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_BACCZ

Accession

Primary (citable) accession number: Q63DJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 25, 2004
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