ID Q9CGB0_LACLA Unreviewed; 346 AA.
AC Q9CGB0;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 104.
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:AAK05286.1};
GN ORFNames=L0038 {ECO:0000313|EMBL:AAK05286.1};
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK05286.1, ECO:0000313|Proteomes:UP000002196};
RN [1] {ECO:0000313|EMBL:AAK05286.1, ECO:0000313|Proteomes:UP000002196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403 {ECO:0000313|EMBL:AAK05286.1,
RC ECO:0000313|Proteomes:UP000002196};
RX PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK05286.1; -; Genomic_DNA.
DR PIR; D86773; D86773.
DR RefSeq; NP_267344.1; NC_002662.1.
DR AlphaFoldDB; Q9CGB0; -.
DR PaxDb; 272623-L0038; -.
DR EnsemblBacteria; AAK05286; AAK05286; L0038.
DR KEGG; lla:L0038; -.
DR PATRIC; fig|272623.7.peg.1275; -.
DR eggNOG; COG3053; Bacteria.
DR HOGENOM; CLU_063190_0_0_9; -.
DR OrthoDB; 9779753at2; -.
DR Proteomes; UP000002196; 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 CDD; cd02169; Citrate_lyase_ligase; 1.
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:AAK05286.1};
KW Lyase {ECO:0000313|EMBL:AAK05286.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Reference proteome {ECO:0000313|Proteomes:UP000002196}.
FT DOMAIN 144..326
FT /note="Citrate lyase ligase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00764"
SQ SEQUENCE 346 AA; 38667 MW; E3A5DD49951B33B2 CRC64;
MLIHRKEWDK FLTDLHLNVS NSSEIETIDE TVAIFAKNGE VLATGSIAGN VIKYVATCTK
GEQSAGERFN KIITELMNRL AQKGIYHVFV FTKPMYAKSF GYLGFKELAR AEQGVLLEKG
RPNITDFLSS LTEKKLVPAG AKKIAAVVMN ANPFTLGHCY LVEQAAAEND FVYVFVVSTD
RSLFRADERL DLVKKGLSAL TNVSVVSGGD YLVSFATFPA YFIQSDEEVM DFQTQIDARI
FKNWFVEALG ITTRYLGAEP FSKTTSIYNQ QLTEVLSDVI DVKIIERKKA DDNEEIISAT
AVRAAIATNQ LEKIRNFVPE TTFEFIEQHL QELQARIKGG QKTNGN
//
