Q729A4 (PANC_DESVH) 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:	DVU_2448

Organism

Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]

Taxonomic identifier

882 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio › Desulfovibrio vulgaris

Protein attributes

Sequence length	283 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. HAMAP-Rule MF_00158
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00158.
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 Reference proteome
Gene Ontology (GO)
Biological_process	pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-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: UniProtKB-HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 283	283	Pantothenate synthetase HAMAP-Rule MF_00158		PRO_0000128226
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)
	Q729A4 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A438BB7446D3BEFB	FASTA	283	31,345
	10 20 30 40 50 60 MQIITEPQTI QQACLRWRAD GVHTALVPTM GYYHAGHESL MAHARAVSEK VIVSLFVNPA 70 80 90 100 110 120 QFGPGEDFAA YPRDLERDAA MAEAQGVDVL FAPKAEDLYK KDHATWVEVP ALSQTMCGLS 130 140 150 160 170 180 RPTHFRGVCT VVTKLLMLTM PRIAVFGQKD WQQVAVIRRM VRDLNIPVDI VGRPIVREPD 190 200 210 220 230 240 GLAMSSRNIY LTAEERLQAP HIHHGLALGR AITQSGERDA ETIKTAIRRY WAQNLPGGEE 250 260 270 280 DYLTIVDPVS LEPVDRLTGA TLCATAVRVG QARLLDNMML LGD

References

[1]

"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. , Haft D.H., Selengut J., Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M. Nat. Biotechnol. 22:554-559(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hildenborough / ATCC 29579 / NCIMB 8303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017285 Genomic DNA. Translation: AAS96920.1.
RefSeq	YP_011660.1. NC_002937.3.
3D structure databases
ProteinModelPortal	Q729A4.
ModBase	Search...
Protein-protein interaction databases
STRING	882.DVU2448.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS96920; AAS96920; DVU_2448.
GeneID	2796625.
KEGG	dvu:DVU2448.
PATRIC	32064508. VBIDesVul119526_2217.
Phylogenomic databases
eggNOG	COG0414.
KO	K01918.
OMA	HLGHITL.
OrthoDB	EOG6Z6FZ4.
ProtClustDB	PRK00380.
Enzyme and pathway databases
BioCyc	DVUL882:GJIL-2504-MONOMER.
UniPathway	UPA00028; UER00005.
Family and domain databases
Gene3D	3.40.50.620. 1 hit.
HAMAP	MF_00158. PanC.
InterPro	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	TIGR00018. panC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PANC_DESVH

Accession

Primary (citable) accession number: Q729A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	July 5, 2004
Last modified:	November 13, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program