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Database: UniProt
Entry: A0A1G5RZ47_9FIRM
LinkDB: A0A1G5RZ47_9FIRM
Original site: A0A1G5RZ47_9FIRM 
ID   A0A1G5RZ47_9FIRM        Unreviewed;       356 AA.
AC   A0A1G5RZ47;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=[Citrate [pro-3S]-lyase] ligase {ECO:0000256|PIRNR:PIRNR005751};
DE            EC=6.2.1.22 {ECO:0000256|PIRNR:PIRNR005751};
GN   ORFNames=SAMN03080599_01731 {ECO:0000313|EMBL:SCZ79394.1};
OS   Acidaminobacter hydrogenoformans DSM 2784.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XII. Incertae Sedis; Acidaminobacter.
OX   NCBI_TaxID=1120920 {ECO:0000313|EMBL:SCZ79394.1, ECO:0000313|Proteomes:UP000199208};
RN   [1] {ECO:0000313|EMBL:SCZ79394.1, ECO:0000313|Proteomes:UP000199208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2784 {ECO:0000313|EMBL:SCZ79394.1,
RC   ECO:0000313|Proteomes:UP000199208};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FMWL01000007; SCZ79394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5RZ47; -.
DR   STRING; 1120920.SAMN03080599_01731; -.
DR   OrthoDB; 9779753at2; -.
DR   Proteomes; UP000199208; 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:SCZ79394.1};
KW   Lyase {ECO:0000313|EMBL:SCZ79394.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR005751};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199208}.
FT   DOMAIN          1..124
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   356 AA;  39499 MW;  AA76D018761FAF65 CRC64;
     MFEERRLRRI EQAEVLLKKC GLKEPVGVDY TMGVFMAPEG RMVATGSLKG DMIQGLAVDP
     EVQGEDLSAK VLTHLINYAI DQGRHTLYLF TKPESAQKLS AVGFRIIAEA KPFASLLEWG
     TTGIDQYVAG LQKLASEDPG EAAAVVVNCN PFTLGHQYLI ETAASRSRKV YVIVVEEDQS
     VFPFEDRIEL VRKGTAHLEN VAVIPGGRYV VSSLTFPSYF TRDSELATAH SAMDVTLFVK
     YIAPALGITK RFVGTEPYSE VTEAYNLAMK AILIPAGVEL EVIERKQLMK GEETHAISAS
     RVRRYIAEGR MEELEDHVPP STFEYLMSIR AFDVIKKLRS SDHTGKGYLE DGSDKQ
//
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