(data stored in SCRATCH zone)

SWISSPROT: PANC_SACEN

ID   PANC_SACEN              Reviewed;         302 AA.
AC   A4F6T0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 78.
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=SACE_0406;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAL99754.1; -; Genomic_DNA.
DR   RefSeq; WP_009946424.1; NZ_PDBV01000001.1.
DR   SMR; A4F6T0; -.
DR   STRING; 405948.SACE_0406; -.
DR   EnsemblBacteria; CAL99754; CAL99754; SACE_0406.
DR   KEGG; sen:SACE_0406; -.
DR   eggNOG; ENOG4107QQT; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; CNHKLEP; -.
DR   OrthoDB; 1661843at2; -.
DR   BioCyc; SERY405948:SACE_RS01995-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000006728; 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; A4F6T0.
DR   SWISS-2DPAGE; A4F6T0.
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..302
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000305542"
FT   NP_BIND         47..54
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   NP_BIND         165..168
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   NP_BIND         202..205
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   ACT_SITE        54
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         79
FT                   /note="Beta-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         79
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         171
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         194
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
SQ   SEQUENCE   302 AA;  32264 MW;  DAB95294C26C3930 CRC64;
     MTAPERVGAG PGFAPGALTV HHHPDELAKV TRALRATGRR ITLVPTMGAL HEGHLELIRR
     ARRDSNSVVV VSIFVNPLQF GPGEDFTSYP RTFETDVEAC RAEGVELVFA PDRDDVYGPD
     PQITVHPGPL GDELEGASRP GHFAGVLTIV AKLLGIVRPD LALFGEKDYQ QLVLIRRMAR
     ELNIDTAIQG IPIVRAPDGL ALSSRNVYLS EEERGAALAL SAALAAGAHA GREGAEAVLR
     AAREVLATEP LVRLDYLELR DTELGAAPAE GEARLLVAAK VGETRLIDNA LVLLGDQGDS
     RP
//

If you have problems or comments...

PBIL Back to PBIL home page