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
//