Reviewed, UniProtKB/Swiss-Prot Q9PIK2 (PANC_CAMJE)

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:	Cj0297c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity.
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP MF_00158
Pathway	Cofactor biosynthesis; pantothenate biosynthesis; pantothenate from beta-alanine and pantoate: step 1/1. HAMAP MF_00158
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential.
Miscellaneous	The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.
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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
flaG	Q0PAW9	1	EBI-1194710,EBI-1191365

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_0000128216
Regions
	Nucleotide binding	30 – 37	8	ATP By similarity
	Nucleotide binding	146 – 149	4	ATP By similarity
	Nucleotide binding	183 – 186	4	ATP By similarity
Sites
	Active site	37	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)
	Q9PIK2-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: C8946F933D7B6475	FASTA	282	32,087
	10 20 30 40 50 60 MQVITSVKEA KQIVKDWKSH QLSIGYVPTM GFLHDGHLSL VKHAKTQDKV IVSIFVNPMQ 70 80 90 100 110 120 FGPNEDFSSY PRDLERDIKM CQDNGVDMVF IPDATQMYLK NFSTYVDMNT ITDKLCGAKR 130 140 150 160 170 180 PGHFRGVCTV LTKFFNILNP DIVYMGQKDA QQCVVVRHMV DDLNFDLKIQ ICPIIREEDG 190 200 210 220 230 240 LAKSSRNVYL SKEERKASLA ISQSIFLAEK LVREGEKNTS KIIQAMKDIL EKEKLIKIDY 250 260 270 280 IELVDFNTME NIENITDNVL GAVAAFVGKT RLIDNFLVQG LK

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL111168 Genomic DNA. Translation: CAL34448.1.
PIR	E81448.
RefSeq	YP_002343735.1.
3D structure databases
HSSP	HSSP built from PDB template 1N2E based on UniProtKB O06280.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PIK2. 31 interactions.
Genome annotation databases
GeneID	904621.
GenomeReviews	Gene locus Cj0297c in contig AL111168_GR.
KEGG	cje:Cj0297c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q9PIK2. SRNVYLN.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0297C-MON.
BRENDA	6.3.2.1. 255835.
Family and domain databases
HAMAP	MF_00158. [Tree]
InterPro	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.
PANTHER	PTHR21299:SF1. Pantoate_ligase. 1 hit.
Pfam	PF02569. Pantoate_ligase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANC_CAMJE

Accession

Primary (citable) accession number: Q9PIK2
Secondary accession number(s): Q0PBL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)