(data stored in ACNUC7421 zone)

SWISSPROT: PANC_RUEPO

ID   PANC_RUEPO              Reviewed;         285 AA.
AC   Q5LWR2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158};
DE            Short=PS {ECO:0000255|HAMAP-Rule:MF_00158};
DE            EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158};
GN   Name=panC {ECO:0000255|HAMAP-Rule:MF_00158};
GN   OrderedLocusNames=SPO0103;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine
CC       in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate +
CC         AMP + diphosphate + H(+); Xref=Rhea:RHEA:10912,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15980, ChEBI:CHEBI:29032,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57966,
CC         ChEBI:CHEBI:456215; EC=6.3.2.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00158};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC       mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00158}.
DR   EMBL; CP000031; AAV93434.1; -; Genomic_DNA.
DR   RefSeq; WP_011045876.1; NC_003911.12.
DR   SMR; Q5LWR2; -.
DR   STRING; 246200.SPO0103; -.
DR   EnsemblBacteria; AAV93434; AAV93434; SPO0103.
DR   KEGG; sil:SPO0103; -.
DR   eggNOG; ENOG4108IAA; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; FVNPSQF; -.
DR   OrthoDB; 1661843at2; -.
DR   BioCyc; RPOM246200:G1G48-104-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00560; PanC; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWR2.
DR   SWISS-2DPAGE; Q5LWR2.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN         1    285       Pantothenate synthetase.
FT                                /FTId=PRO_0000305555.
FT   NP_BIND      32     39       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     149    152       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     186    189       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     39     39       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING      63     63       Beta-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING      63     63       Pantoate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING     155    155       Pantoate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING     178    178       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
SQ   SEQUENCE   285 AA;  30411 MW;  1E87D9953E657AD8 CRC64;
     MSAPILRKLA DLRAATAGWK RAGESIGVVP TMGALHDGHL SLVAAAKAGC DRVVVTIFVN
     PKQFNNPEDL AKYPRTELAD ASKLAPYGVD AIYVPDPDQI YPEGFATTVS VSGLTDVMEG
     ACRPGHFDGV ATVVAKLFLQ TGADQAYFGE KDYQQMMLVT RMAQDLDIPI TVVGCPTVRE
     ASGLAMSSRN MRLSAEGLER AGRLHPVMRQ VAERLAAGAS FGDLAPGARE ALGAAGFVDI
     EYFDLRAADS LRALDRPTEP ARLLVAAWLD GVRLIDNIAV SQLND
//

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