ID A0A2M8TH88_9CLOT Unreviewed; 346 AA.
AC A0A2M8TH88;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:PJI10355.1};
GN ORFNames=CUB90_11910 {ECO:0000313|EMBL:PJI10355.1};
OS Clostridium sp. CT7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2052574 {ECO:0000313|EMBL:PJI10355.1, ECO:0000313|Proteomes:UP000230839};
RN [1] {ECO:0000313|EMBL:PJI10355.1, ECO:0000313|Proteomes:UP000230839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT7 {ECO:0000313|EMBL:PJI10355.1,
RC ECO:0000313|Proteomes:UP000230839};
RA Xin F., Chen T.;
RT "The draft genome sequence of Clostridium sp. CT7, a unique bacterium
RT capable of producing butanol from glycerol uncoupled acetone and 1,3-
RT propanediol formation.";
RL Submitted (NOV-2017) 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:PJI10355.1}.
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DR EMBL; PETE01000002; PJI10355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8TH88; -.
DR OrthoDB; 9779753at2; -.
DR Proteomes; UP000230839; 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; 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:PJI10355.1};
KW Lyase {ECO:0000313|EMBL:PJI10355.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Reference proteome {ECO:0000313|Proteomes:UP000230839}.
FT DOMAIN 1..132
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 346 AA; 40165 MW; 000803D2C1B5E832 CRC64;
MAAEYLSLQE EIIDSRDLKR LQEVEQFLLK QGLRFDKNVE YTIAIYEEDK IIGTGSFEGR
ILKCIAVDGR YRGMGISNKI ISQLVSEEYR RGNSHIFIYT KPKNYKMFSD MGFYKVAQVT
DKVLLLENDP LGIYKFVEKL KRKKVEGRVV SALVMNCNPF TLGHKYLIEK ASRESDVVHV
FIVWENKSVF PSDVRYKLAR KGVQHLNNVV FHKGEDYVIS SATFPSYFIK KQNEVARIQS
LLDVQIFIKY IIPALGITRR YVGEEPFCDV TRTYNNVMKE ILPTRGIEIM EISRLSINEE
VISASKVRKL IKEKKLLYVK DLVPDTTYRF LCSKEALPII NKIQNK
//
