ID   CITC_LEUMC              Reviewed;         338 AA.
AC   O53076;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=[Citrate [pro-3S]-lyase] ligase;
DE            EC=6.2.1.22;
DE   AltName: Full=Acetate:SH-citrate lyase ligase;
DE   AltName: Full=Citrate lyase synthetase;
GN   Name=citC;
OS   Leuconostoc mesenteroides subsp. cremoris.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=33965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=195;
RX   PubMed=9457870; DOI=10.1128/jb.180.3.647-654.1998;
RA   Bekal S., van Beeumen J., Samyn B., Garmyn D., Henini S., Divies C.,
RA   Prevost H.;
RT   "Purification of Leuconostoc mesenteroides citrate lyase and cloning and
RT   characterization of the citCDEFG gene cluster.";
RL   J. Bacteriol. 180:647-654(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Bekal S.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-
CC       dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate
CC         lyase ACP] + AMP + diphosphate; Xref=Rhea:RHEA:23788, Rhea:RHEA-
CC         COMP:10158, Rhea:RHEA-COMP:13710, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82683,
CC         ChEBI:CHEBI:137976, ChEBI:CHEBI:456215; EC=6.2.1.22;
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DR   EMBL; Y10621; CAA71636.1; -; Genomic_DNA.
DR   AlphaFoldDB; O53076; -.
DR   GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR005216; Citrate_lyase_ligase.
DR   InterPro; IPR013166; Citrate_lyase_ligase_C.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR40599; PTHR40599; 1.
DR   Pfam; PF08218; Citrate_ly_lig; 1.
DR   PIRSF; PIRSF005751; Acet_citr_lig; 1.
DR   SMART; SM00764; Citrate_ly_lig; 1.
DR   TIGRFAMs; TIGR00124; cit_ly_ligase; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..338
FT                   /note="[Citrate [pro-3S]-lyase] ligase"
FT                   /id="PRO_0000089773"
SQ   SEQUENCE   338 AA;  38460 MW;  0CDD5A6D0E4731C1 CRC64;
     MRRDWQNFLM ACGIKNFDDS ELNPLDITIA VYENEEIIGT GSIAGDVIKY VAVQETTMSG
     HSTLFNQLMT KLENFMAVEG RFHQFVLRNQ FTKKVLNTLA SKRWLSVNKE FCWKKDYQIL
     RNTCQQFPSQ TPIDKVASVV INANPFTNGH RFLIEEASRN NELVYVFVLN QEASLFHTDE
     RIALVKAGVQ DLSNVIVVNG GAYIISYLTF PAYFLKHNDS AIDYQTTIDV RLFKYKIASA
     LGITSRYVGS EPLSHTTNLY NQKLISELNP QIEVHVIQRK LAAGDLGVIS ARTVREAIDK
     GDEAVWQKMV TETTQHFISN NLLELQQRIR KGQKINGN