Reviewed, UniProtKB/Swiss-Prot Q9X713 (PANC_CORGL)

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:	Cgl0113, cg0148

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
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. Ref.1
Catalytic activity	ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. Ref.1
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: 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 – 279	279	Pantothenate synthetase HAMAP MF_00158		PRO_0000128224
Regions
	Nucleotide binding	26 – 33	8	ATP By similarity
	Nucleotide binding	147 – 150	4	ATP By similarity
	Nucleotide binding	184 – 187	4	ATP By similarity
Sites
	Active site	33	1	Proton donor By similarity
	Binding site	57	1	Beta-alanine By similarity
	Binding site	57	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)
	Q9X713-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: EE4CF5EB4198A768	FASTA	279	29,888
	10 20 30 40 50 60 MQVATTKQAL IDALLHHKSV GLVPTMGALH SGHASLVKAA RAENDTVVAS IFVNPLQFEA 70 80 90 100 110 120 LGDCDDYRNY PRQLDADLAL LEEAGVDIVF APDVEEMYPG GLPLVWARTG SIGTKLEGAS 130 140 150 160 170 180 RPGHFDGVAT VVAKLFNLVR PDRAYFGQKD AQQVAVIRRL VADLDIPVEI RPVPIIRGAD 190 200 210 220 230 240 GLAESSRNQR LSADQRAQAL VLPQVLSGLQ RRKAAGEALD IQGARDTLAS ADGVRLDHLE 250 260 270 IVDPATLEPL EIDGLLTQPA LVVGAIFVGP VRLIDNIEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"D-pantothenate synthesis in Corynebacterium glutamicum and use of panBC and genes encoding L-valine synthesis for D-pantothenate overproduction." Eggeling L., Sahm H. Appl. Environ. Microbiol. 65:1973-1979(1999) [PubMed: 10223988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X96580 Genomic DNA. Translation: CAA65398.1. BA000036 Genomic DNA. Translation: BAB97506.1. BX927148 Genomic DNA. Translation: CAF18681.1.
PIR	T47120.
RefSeq	NP_599366.1. YP_224410.1.
3D structure databases
SMR	Q9X713. Positions 1-279.
ModBase	Search...
Genome annotation databases
GeneID	1021074. 3343643.
GenomeReviews	Gene locus Cgl0113 in contig BA000036_GR.
KEGG	cgb:cg0148. cgl:NCgl0112.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG428839.
OMA	MPIQIIG.
PhylomeDB	Q9X713.
Enzyme and pathway databases
BioCyc	CGLU196627:CG0148-MONOMER.
BRENDA	6.3.2.1. 812.
Family and domain databases
HAMAP	MF_00158. PanC. [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_CORGL

Accession

Primary (citable) accession number: Q9X713

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	February 9, 2010
This is version 60 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)