Q18C33 (PANC_CLOD6) 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:	CD630_15120

Organism

Clostridium difficile (strain 630) [Complete proteome] [HAMAP]

Taxonomic identifier

272563 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Clostridium difficile

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-Rule MF_00158
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00158.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP-Rule 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: HAMAP
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: HAMAP
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-Rule MF_00158		PRO_0000305426
Regions
	Nucleotide binding	29 – 36	8	ATP By similarity
	Nucleotide binding	146 – 149	4	ATP By similarity
	Nucleotide binding	183 – 186	4	ATP By similarity
Sites
	Active site	36	1	Proton donor By similarity
	Binding site	60	1	Beta-alanine By similarity
	Binding site	60	1	Pantoate By similarity
	Binding site	152	1	Pantoate By similarity
	Binding site	175	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q18C33 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: E18317B71E2DBF8C	FASTA	282	31,691
	10 20 30 40 50 60 MLVKEIKLLR NIIKDWRKHG YSIGLVTTMG FLHEGHQSLI KKAVKENDKV VVSVFVNPTQ 70 80 90 100 110 120 FGPNEDFNSY PRDIDKDFKY CMDSGATVVF NPSPEEMYLK GNCTTINVSG LTDFLCGAKR 130 140 150 160 170 180 PVHFGGVCLV VSKFLNIVTP DKAYFGEKDA QQLAVIKRMV KDLNIDTEII GCPIIRENDG 190 200 210 220 230 240 LAKSSRNTYL SEEERKSALI LNKSLSLAKE ELVKGNLNPE NIKELITAKI NSEHLAKIDY 250 260 270 280 VEIVDSETLQ PVKQIEHSIL VAIAVFIGKT RLIDNFTFEL NI

References

[1]

"The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome." Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., Brooks K., Chillingworth T. , Cronin A., Davis P., Dowd L., Fraser A., Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J. Nat. Genet. 38:779-786(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 630.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM180355 Genomic DNA. Translation: CAJ68377.1.
RefSeq	YP_001088013.1. NC_009089.1.
3D structure databases
ProteinModelPortal	Q18C33.
SMR	Q18C33. Positions 3-277.
ModBase	Search...
Protein-protein interaction databases
STRING	272563.CD1512.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ68377; CAJ68377; CD630_15120.
GeneID	4916551.
KEGG	cdf:CD630_15120.
PATRIC	19441397. VBICloDif38397_1586.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HOG000175517.
KO	K01918.
OMA	HTIVSVF.
ProtClustDB	PRK00380.
Enzyme and pathway databases
BioCyc	CDIF272563:GJFE-1684-MONOMER.
UniPathway	UPA00028; UER00005.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_00158. PanC.
InterPro	IPR004821. Cyt_trans-like. IPR003721. Pantoate_ligase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
PANTHER	PTHR21299:SF1. PTHR21299:SF1. 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_CLOD6

Accession

Primary (citable) accession number: Q18C33

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	July 25, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program