(data stored in ACNUC1104 zone)

SWISSPROT: PANC_NOCSJ

ID   PANC_NOCSJ              Reviewed;         334 AA.
AC   A1SDW7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 68.
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=Noca_0460;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000509; ABL80002.1; -; Genomic_DNA.
DR   RefSeq; WP_011753953.1; NC_008699.1.
DR   SMR; A1SDW7; -.
DR   STRING; 196162.Noca_0460; -.
DR   EnsemblBacteria; ABL80002; ABL80002; Noca_0460.
DR   KEGG; nca:Noca_0460; -.
DR   eggNOG; ENOG4107QQT; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; FVNPSQF; -.
DR   OrthoDB; 1661843at2; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000000640; 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; 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; TIGR00018; panC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDW7.
DR   SWISS-2DPAGE; A1SDW7.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN         1    334       Pantothenate synthetase.
FT                                /FTId=PRO_0000305501.
FT   NP_BIND      34     41       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     158    161       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     195    198       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     41     41       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING      71     71       Beta-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING      71     71       Pantoate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING     164    164       Pantoate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING     187    187       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
SQ   SEQUENCE   334 AA;  35428 MW;  F768B1F398A15688 CRC64;
     MSSAPVLAHT REELATLLAA ARARGEQVGL VPTMGALHEG HASLVRAARE RVTDDGRMGP
     VVVSVFVNPL QFGANEDLDR YPRTLEADLE VCAREGADIV FAPSVDEVYP GGPPQVTVRP
     GPLGKILEGK VRPGHFRGVL TVVAKLFGLV RPDVAVFGQK DYQQLALIRR MVLDLALGVE
     IVAAETVRED DGLALSSRNR YLEPEQREQA VALSRALLAA QENAGYGAEV ALDEARAELR
     AAPGVDLDYL VITDPDLDEL PAVVPPGTPA RILVAARVGG TRLIDNLPLM LGTRGPAGEA
     SPPNRERSEP GSAEQNKSPG EARTTPSGTS EASE
//

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