(data stored in ACNUC7421 zone)

SWISSPROT: PANC_RHILO

ID   PANC_RHILO              Reviewed;         283 AA.
AC   Q98ND0;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 92.
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=mll0196;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB47831.1; -; Genomic_DNA.
DR   RefSeq; WP_010909201.1; NC_002678.2.
DR   SMR; Q98ND0; -.
DR   STRING; 266835.14021218; -.
DR   EnsemblBacteria; BAB47831; BAB47831; BAB47831.
DR   KEGG; mlo:mll0196; -.
DR   PATRIC; fig|266835.9.peg.152; -.
DR   eggNOG; ENOG4107R03; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; CNHKLEP; -.
DR   OrthoDB; 1661843at2; -.
DR   BioCyc; MLOT266835:G1G20-151-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000000552; 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; IPR004821; Cyt_trans-like.
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; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q98ND0.
DR   SWISS-2DPAGE; Q98ND0.
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis.
FT   CHAIN           1..283
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000128261"
FT   NP_BIND         33..40
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   NP_BIND         150..153
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   NP_BIND         187..190
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   ACT_SITE        40
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         64
FT                   /note="Beta-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         64
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         156
FT                   /note="Pantoate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         179
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
SQ   SEQUENCE   283 AA;  30756 MW;  619B61AB91F3EF83 CRC64;
     MSRPEVVNSV AALRAQVSDW RRDGLRVAMV PTMGALHEGH LSLIRIAREK AERCVVSIFV
     NPTQFAPSED LDKYPRQLAR DLDLLARVKA DLAFTPTVGA MYPAGFATRI SVGGPSAGLE
     SDFRPTFFEG VATVVAKLFL QATPDCAVFG EKDYQQLCVV RQLCRDLDLP VEIIGAPTIR
     DAHGLAMSSR NAYLDEAELA VARRLNVILH KAAAALAAGT HQDDATGEAN RALIAAGFQK
     IDYVEARESL TLAPWRRDRA GRVLAAAWLG KTRLIDNVDV PVA
//

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