Q9RV66 (PANC_DEIRA) 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:	DR_1164

Organism

Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]

Taxonomic identifier

243230 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › Deinococcus radiodurans

Protein attributes

Sequence length	281 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 Reference 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 – 281	281	Pantothenate synthetase HAMAP-Rule MF_00158		PRO_0000128225
Regions
	Nucleotide binding	17 – 24	8	ATP By similarity
	Nucleotide binding	134 – 137	4	ATP By similarity
	Nucleotide binding	176 – 179	4	ATP By similarity
Sites
	Active site	24	1	Proton donor By similarity
	Binding site	48	1	Beta-alanine By similarity
	Binding site	48	1	Pantoate By similarity
	Binding site	140	1	Pantoate By similarity
	Binding site	163	1	ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RV66 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 91112B0C2B9AEDA8	FASTA	281	30,118
	10 20 30 40 50 60 MQTALASRGR VGLVPTMGFL HEGHATLIRR ARAECDVVVV SIFVNPMQFG PTEDLATYPR 70 80 90 100 110 120 DLDRDLALAG AAGADFVFHP EAAAMYPAGF STRVEVSGVS EPLDGAARPG HFAGVATVVL 130 140 150 160 170 180 KLLNIVQPER AYFGEKDWQQ LAVVRRLVAD LNLRSEIVGV PTVRADEEAA HAGLALSSRN 190 200 210 220 230 240 SYLSPEQQRR ATVLSRALRA VQAAYAGGER DTGRLRQAGL DVLASEPELA LDYLVVVGPD 250 260 270 280 LRDVPQLSDD PLNRVLIAGR LFGVRLIDNM PLSTAPVPAP A

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF10737.1.
PIR	G75430.
RefSeq	NP_294888.1. NC_001263.1.
3D structure databases
ProteinModelPortal	Q9RV66.
SMR	Q9RV66. Positions 8-273.
ModBase	Search...
Protein-protein interaction databases
STRING	243230.DR_1164.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF10737; AAF10737; DR_1164.
GeneID	1800443.
KEGG	dra:DR_1164.
PATRIC	21629922. VBIDeiRad64572_1362.
Phylogenomic databases
eggNOG	COG0414.
HOGENOM	HOG000175516.
KO	K01918.
OMA	AIIREMV.
ProtClustDB	PRK00380.
Enzyme and pathway databases
BioCyc	DRAD243230:GH46-1534-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_DEIRA

Accession

Primary (citable) accession number: Q9RV66

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program