ID A0A3P1W859_9FUSO Unreviewed; 338 AA.
AC A0A3P1W859;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:RRD40693.1};
GN ORFNames=EII29_01815 {ECO:0000313|EMBL:RRD40693.1};
OS Leptotrichia sp. OH3620_COT-345.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=2491048 {ECO:0000313|EMBL:RRD40693.1, ECO:0000313|Proteomes:UP000280115};
RN [1] {ECO:0000313|EMBL:RRD40693.1, ECO:0000313|Proteomes:UP000280115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH3620_COT-345 {ECO:0000313|EMBL:RRD40693.1,
RC ECO:0000313|Proteomes:UP000280115};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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 {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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRD40693.1}.
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DR EMBL; RQYW01000002; RRD40693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1W859; -.
DR OrthoDB; 9779753at2; -.
DR Proteomes; UP000280115; Unassembled WGS sequence.
DR GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR005216; Citrate_lyase_ligase.
DR InterPro; IPR013166; Citrate_lyase_ligase_C.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR000182; GNAT_dom.
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; PF13673; Acetyltransf_10; 1.
DR Pfam; PF08218; Citrate_ly_lig; 1.
DR PIRSF; PIRSF005751; Acet_citr_lig; 1.
DR SMART; SM00764; Citrate_ly_lig; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Ligase {ECO:0000256|PIRNR:PIRNR005751, ECO:0000313|EMBL:RRD40693.1};
KW Lyase {ECO:0000313|EMBL:RRD40693.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751}.
FT DOMAIN 1..123
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 338 AA; 39104 MW; 261D9F9CDEEEAFAE CRC64;
MNVSKLDYKN SFELRELKEF LEKFELEFDS SVDYTAVIRE NEEIIATVSK DRNIIKDFAV
DKSHQGKGLS NILLTEIRNK LVEEGYLSSM IFTKIENKFI FEDMGYKKVA CTDKVILLEQ
GNEDIEGIIS NIIKNNNLDI RHKRAMIVMN CNPFTLGHRY LIENAAKNNN EVIIFVLEEN
KSTFSFKTRI QLVKKGTEDL KNVKVVPSTK YIISSATFPS YFLKDKNSML TEYAKLDSEI
IATKFCRRLN INHRYLGEEP FDEVTSVYNR IISEILPKYG IEVNIIPRKS IDGKIISASS
VRKLLKEGKM EEIRKIVPYT TFEYLDSLKN KEISGKLK
//
