(data stored in ACNUC7421 zone)

SWISSPROT: PANC_SHISS

ID   PANC_SHISS              Reviewed;         283 AA.
AC   Q3Z5M7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 82.
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=SSON_0141;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ86935.1; -; Genomic_DNA.
DR   SMR; Q3Z5M7; -.
DR   EnsemblBacteria; AAZ86935; AAZ86935; SSON_0141.
DR   KEGG; ssn:SSON_0141; -.
DR   HOGENOM; HOG000175517; -.
DR   KO; K01918; -.
DR   OMA; FVNPSQF; -.
DR   BioCyc; SSON300269:G1GL2-159-MONOMER; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000002529; 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; IPR004821; Cyt_trans-like.
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; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z5M7.
DR   SWISS-2DPAGE; Q3Z5M7.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis.
FT   CHAIN         1    283       Pantothenate synthetase.
FT                                /FTId=PRO_0000305554.
FT   NP_BIND      30     37       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     149    152       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     186    189       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   ACT_SITE     37     37       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING      61     61       Beta-alanine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING      61     61       Pantoate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING     155    155       Pantoate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
SQ   SEQUENCE   283 AA;  31550 MW;  575364697C1AFB20 CRC64;
     MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV VVVSIFVNPM
     QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP NGTETHTYVD VPGLSTMLEG
     ASRPGHFRGV STIVSKLFNL VQPDIACFGE KDFQQLALIR KMVADMGFDI EIVGVPIMRA
     KDGLALSSRN GYLTAEQRKI APGLYKVLSS IADKLQAGER DLDEIIAIAG QELNEKGFRA
     DDIQIRDADT LLEVSETSKR AVILVAAWLG DARLIDNKIV ELA
//

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