(data stored in ACNUC29543 zone)

SWISSPROT: PANC_ACIBT

ID   PANC_ACIBT              Reviewed;         282 AA.
AC   A3M294;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAY-2019, entry version 72.
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=A1S_0587;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 /
OS   NCDC KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by
RT   high-density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO11038.2; -; Genomic_DNA.
DR   SMR; A3M294; -.
DR   EnsemblBacteria; ABO11038; ABO11038; A1S_0587.
DR   KEGG; acb:A1S_0587; -.
DR   HOGENOM; HOG000175517; -.
DR   KO; K01918; -.
DR   UniPathway; UPA00028; UER00005.
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; A3M294.
DR   SWISS-2DPAGE; A3M294.
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis.
FT   CHAIN         1    282       Pantothenate synthetase.
FT                                /FTId=PRO_0000305385.
FT   NP_BIND      30     37       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     148    151       ATP. {ECO:0000255|HAMAP-Rule:MF_00158}.
FT   NP_BIND     185    188       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     154    154       Pantoate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
FT   BINDING     177    177       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00158}.
SQ   SEQUENCE   282 AA;  31066 MW;  91C5D0EDFF14C657 CRC64;
     MKTETTIQGL AASLNPARAA RKIIGFVPTM GNLHEGHLTL VREAKKLCDV VVVSIFVNPT
     QFGPGEDFDN YPRTLEQDSR LLADVGCDII FAPSVEQMYG TQPRLTNISV SQITDDLCGS
     SRPGHFDGVA LVVTKLFNIV QPNYAFFGQK DYQQLAVIRQ FVQDLNIPLE VIGVPIVRAE
     DGLALSSRNG YLTPEQRQVA PVIYQGLKQA EEQLHQGKDL QQVLADLKTL LTDNGFVVDY
     VEARQPNLLA ASQFDRDIVL FVAAKLGGTR LIDNLQVAFT PQ
//

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