(data stored in SCRATCH zone)

SWISSPROT: C0ZPL3_RHOE4

ID   C0ZPL3_RHOE4            Unreviewed;       313 AA.
AC   C0ZPL3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Pantothenate synthetase {ECO:0000256|HAMAP-Rule:MF_00158};
DE            Short=PS {ECO:0000256|HAMAP-Rule:MF_00158};
DE            EC=6.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate--beta-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00158};
DE   AltName: Full=Pantoate-activating enzyme {ECO:0000256|HAMAP-Rule:MF_00158};
GN   Name=panC {ECO:0000256|HAMAP-Rule:MF_00158,
GN   ECO:0000313|EMBL:BAH31341.1};
GN   OrderedLocusNames=RER_06330 {ECO:0000313|EMBL:BAH31341.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31341.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31341.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine
CC       in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC       {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00158, ECO:0000256|SAAS:SAAS01125062};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00158, ECO:0000256|SAAS:SAAS00094317}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158,
CC       ECO:0000256|SAAS:SAAS00573540}.
CC   -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC       mechanism. {ECO:0000256|HAMAP-Rule:MF_00158}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00158, ECO:0000256|SAAS:SAAS00921032}.
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DR   EMBL; AP008957; BAH31341.1; -; Genomic_DNA.
DR   RefSeq; WP_020906076.1; NC_012490.1.
DR   STRING; 234621.RER_06330; -.
DR   EnsemblBacteria; BAH31341; BAH31341; RER_06330.
DR   KEGG; rer:RER_06330; -.
DR   PATRIC; fig|234621.6.peg.1080; -.
DR   eggNOG; ENOG4108IAA; Bacteria.
DR   eggNOG; COG0414; LUCA.
DR   HOGENOM; HOG000175516; -.
DR   KO; K01918; -.
DR   OMA; FVNPSQF; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002204; 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; C0ZPL3.
DR   SWISS-2DPAGE; C0ZPL3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464754};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464734};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464803, ECO:0000313|EMBL:BAH31341.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464749};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00158,
KW   ECO:0000256|SAAS:SAAS00464740}.
FT   NP_BIND      45     52       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     162    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   NP_BIND     199    202       ATP. {ECO:0000256|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     52     52       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      76     76       Beta-alanine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING      76     76       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     168    168       Pantoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
FT   BINDING     191    191       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00158}.
SQ   SEQUENCE   313 AA;  33318 MW;  B2CF4E1480E0E85F CRC64;
     MTVVSDLQGG YKRGELTVHH DPDRLRRVSR ALRGVGRQVA LVPTMGALHA GHIELVRQAK
     VTGAVVIVSI FVNPLQFGAG EDLDAYPRTL DADLDLLRAE GVELVFAPSA KTMYPRGQRT
     TIVPGPLGSE LEGGARPTHF AGMLTVVAKL LQIAAPNHAY FGEKDYQQLT LIRQMVWDLN
     FDVQIIGVPT VREFDGLALS SRNRYLDEGQ RAAAVALSAA LIAGAHAASG GAEAILETAR
     AVLAAVPEIE VDYLEVRGVD LGPAPERGDG RLLVAAKLGT TRLIDNVGVA VGTGFLERDT
     DPSADAIDDL LSH
//

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