ID H5UQU0_9MICO Unreviewed; 356 AA.
AC H5UQU0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:GAB48098.1};
GN ORFNames=MOPEL_060_00140 {ECO:0000313|EMBL:GAB48098.1};
OS Mobilicoccus pelagius NBRC 104925.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Mobilicoccus.
OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB48098.1, ECO:0000313|Proteomes:UP000004367};
RN [1] {ECO:0000313|EMBL:GAB48098.1, ECO:0000313|Proteomes:UP000004367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB48098.1,
RC ECO:0000313|Proteomes:UP000004367};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL Submitted (FEB-2012) 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:GAB48098.1}.
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DR EMBL; BAFE01000043; GAB48098.1; -; Genomic_DNA.
DR RefSeq; WP_009481996.1; NZ_BAFE01000043.1.
DR AlphaFoldDB; H5UQU0; -.
DR STRING; 1089455.MOPEL_060_00140; -.
DR eggNOG; COG3053; Bacteria.
DR Proteomes; UP000004367; 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; IPR000182; GNAT_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00124; cit_ly_ligase; 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:GAB48098.1};
KW Lyase {ECO:0000313|EMBL:GAB48098.1};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751};
KW Reference proteome {ECO:0000313|Proteomes:UP000004367}.
FT DOMAIN 1..129
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 356 AA; 39559 MW; 84143A973E16D8AB CRC64;
MIHEIDLSTV SPAAHPEEMD EIRRFLAAHD LDLDTTLEVV VTARHYGTLL GCAGLTGDVV
KCVAVAEEMQ GHDLLPRLML EVSFLALDRG HPHLFLYTSP RNETAFRACG FHPIVTVPDQ
VLMMENTPRG VHAYAEELRS YRRERERVGA VVLNANPFTL GHRHLLTRAA SECDYLHVFV
VGEDSSAFPF AQRLALVREG VSEMDLRDRI HVHPGTRYVV SKATFPTYFI KDRGIVDLVA
TAVDLLVFRQ HIAPSLGVTH RYVGTEPFCT VTRQYNADMH YWLERRDLPA PPIEVVEIPR
LERGGAAISA TEVRRRLAAG DLDGLRPLVP RPTWQLLTSS PASARALAPS PTSGGA
//