(data stored in SCRATCH 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   11-DEC-2019, entry version 71.
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}; 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., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   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 in
CC       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 + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00158};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       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; CNHKLEP; -.
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; 3.30.1300.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR042176; Pantoate_ligase_C.
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; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000305501"
FT   NP_BIND         34..41
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   NP_BIND         158..161
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   NP_BIND         195..198
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   ACT_SITE        41
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         71
FT                   /note="Beta-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         71
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         164
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         187
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-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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