ID B1MWL8_LEUCK Unreviewed; 351 AA.
AC B1MWL8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=[Citrate [pro-3S]-lyase] ligase {ECO:0000256|PIRNR:PIRNR005751};
DE EC=6.2.1.22 {ECO:0000256|PIRNR:PIRNR005751};
GN Name=citC {ECO:0000313|EMBL:ACA81940.1};
GN OrderedLocusNames=LCK_00107 {ECO:0000313|EMBL:ACA81940.1};
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA81940.1, ECO:0000313|Proteomes:UP000002166};
RN [1] {ECO:0000313|EMBL:ACA81940.1, ECO:0000313|Proteomes:UP000002166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20 {ECO:0000313|EMBL:ACA81940.1,
RC ECO:0000313|Proteomes:UP000002166};
RX PubMed=18281406; DOI=10.1128/JB.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
CC -!- FUNCTION: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-
CC dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
CC {ECO:0000256|PIRNR:PIRNR005751}.
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;
CC Evidence={ECO:0000256|PIRNR:PIRNR005751};
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DR EMBL; DQ489736; ACA81940.1; -; Genomic_DNA.
DR RefSeq; WP_004908613.1; NC_010471.1.
DR AlphaFoldDB; B1MWL8; -.
DR STRING; 349519.LCK_00107; -.
DR KEGG; lci:LCK_00107; -.
DR eggNOG; COG3053; Bacteria.
DR HOGENOM; CLU_063190_0_0_9; -.
DR OrthoDB; 9779753at2; -.
DR Proteomes; UP000002166; Chromosome.
DR GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00124; cit_ly_ligase; 1.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR40599; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR PANTHER; PTHR40599:SF1; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR Pfam; PF08218; Citrate_ly_lig; 1.
DR PIRSF; PIRSF005751; Acet_citr_lig; 1.
DR SMART; SM00764; Citrate_ly_lig; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Ligase {ECO:0000256|PIRNR:PIRNR005751, ECO:0000313|EMBL:ACA81940.1};
KW Lyase {ECO:0000313|EMBL:ACA81940.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751}.
FT DOMAIN 151..331
FT /note="Citrate lyase ligase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00764"
SQ SEQUENCE 351 AA; 39492 MW; 13069293F51A7AD7 CRC64;
MADIIRDINL NNPTQRQYWQ TFLSELDIDN FNEKELIGIE KIVGLFDGER LVGTGAIAGK
VLKYIAVCDR GATSKGARFN QVMTTLENYM ATLGRFHHFV FTKPRYIASF KHIGFGVLAE
SSLGAILEKG LPDVHSFIRQ LPQMGNQTSR IAAVIVNANP FTRGHRYLIE KAATENDFVY
VFVVAQDVSL FTTAERQMLV SKGVADLKNV VVVSGGDYMV SYLTFPSYFI HDETTVIDYQ
TTLDARLFKN IIAPARHITR RYVGSEPLSE TTAHYNQTLA REFDDSIELT IVPRLNSQRQ
VVSARAVREA IATDNRQVWT EMVPETTALF ISENITALQT RIRKGQKIDG N
//
