Reviewed, UniProtKB/Swiss-Prot Q6HL15 (PANC_BACHK)

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:	BT9727_1422

Organism

Bacillus thuringiensis subsp. konkukian [Complete proteome] [HAMAP]

Taxonomic identifier

180856 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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
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_0000128205
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)
	Q6HL15-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: C2081E04BCBD53D9	FASTA	282	31,963
	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 VADFNIPVII VPVDIVREED 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: 97-27.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017355 Genomic DNA. Translation: AAT63199.1.
RefSeq	YP_035756.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2858358.
GenomeReviews	Gene locus BT9727_1422 in contig AE017355_GR.
KEGG	btk:BT9727_1422.
NMPDR	fig|281309.1.peg.1396.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6HL15.
OMA	VADFNIP.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_1422-MON.
Family and domain databases
HAMAP	MF_00158. [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.
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_BACHK

Accession

Primary (citable) accession number: Q6HL15

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 33 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)