ID A0A7K4AGC1_METSH Unreviewed; 622 AA. AC A0A7K4AGC1; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 22-FEB-2023, entry version 8. DE SubName: Full=ATP citrate synthase {ECO:0000313|EMBL:NLJ21999.1}; GN ORFNames=GX426_02680 {ECO:0000313|EMBL:NLJ21999.1}; OS Methanothrix soehngenii (Methanosaeta concilii). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanotrichales; Methanotrichaceae; Methanothrix. OX NCBI_TaxID=2223 {ECO:0000313|EMBL:NLJ21999.1, ECO:0000313|Proteomes:UP000544742}; RN [1] {ECO:0000313|EMBL:NLJ21999.1, ECO:0000313|Proteomes:UP000544742} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS27yjCOA_157 {ECO:0000313|EMBL:NLJ21999.1}; RX PubMed=32123542; RA Campanaro S., Treu L., Rodriguez-R L.M., Kovalovszki A., Ziels R.M., RA Maus I., Zhu X., Kougias P.G., Basile A., Luo G., Schluter A., RA Konstantinidis K.T., Angelidaki I.; RT "New insights from the biogas microbiome by comprehensive genome-resolved RT metagenomics of nearly 1600 species originating from multiple anaerobic RT digesters."; RL Biotechnol. Biofuels 13:25-20(2020). RN [2] {ECO:0007829|PDB:6ZNW} RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS). RX PubMed=34294920; DOI=10.1038/s41594-021-00624-3; RA Verstraete K., Verschueren K.H.G., Dansercoer A., Savvides S.N.; RT "Acetyl-CoA is produced by the citrate synthase homology module of ATP- RT citrate lyase."; RL Nat. Struct. Mol. Biol. 28:636-638(2021). CC -!- CATALYTIC ACTIVITY: CC Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate; CC Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:456216; EC=6.2.1.13; CC Evidence={ECO:0000256|ARBA:ARBA00001619}; 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:NLJ21999.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAAYUN010000049; NLJ21999.1; -; Genomic_DNA. DR PDB; 6ZNW; X-ray; 2.12 A; B=1-622. DR AlphaFoldDB; A0A7K4AGC1; -. DR SMR; A0A7K4AGC1; -. DR Proteomes; UP000544742; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR CDD; cd06100; CCL_ACL-C; 1. DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1. DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1. DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub. DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub. DR InterPro; IPR002020; Citrate_synthase. DR InterPro; IPR036969; Citrate_synthase_sf. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1. DR PANTHER; PTHR23118:SF42; ATP-CITRATE SYNTHASE; 1. DR Pfam; PF00285; Citrate_synt; 1. DR Pfam; PF02629; CoA_binding; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PRINTS; PR01798; SCOASYNTHASE. DR SUPFAM; SSF48256; Citrate synthase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:6ZNW}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}. FT DOMAIN 12..115 FT /note="CoA-binding" FT /evidence="ECO:0000259|Pfam:PF02629" FT DOMAIN 175..299 FT /note="ATP-citrate lyase/succinyl-CoA ligase" FT /evidence="ECO:0000259|Pfam:PF00549" SQ SEQUENCE 622 AA; 68078 MW; 9B219E8BDED3958E CRC64; MSRKDYVLFD INTKAFVYGY QTNAIQRMLD FDYVCKRSSP SISAIINPSR AGIHKAFWGT KEIILPMYKT IPLAALAYPE ADVMVNFASH RSAFETTMEA LQEDTIRIVA VIAEGVPERQ SRVMAATARK LDKIVIGPAT VGGMTAGAFR IGNTAGTIEN IIASKLYRPG CVGFVSKSGG MLNEAFNIIS RNSDGIYEGV AIGGDRYPGS NMLDHILRYE RNPAIKMIAC LGELGGEDEY MIIQALKEKK ITKPLVAWVT GTCSPYLPAS VQFGHAGAKA NTEKETAQAK NDAFRQAGAY VPRSFDDYGE MVRQVYDMLL TRGIVQKFDE PEVPRIPTDY SKALATGDIR KPTTFICTIS DDSGEELLYA GKKLSDVLDR KMGIGGVIGL LWFKKELPEY AAHFIELVIQ IVADHGPAVS GAHNAIVASC AGKDLISSLC SGLLTIGPRF GGAIDDAARE FKRAQETGLA PEQFVGEMKK KGINIPGIGH KIKSVKNPDK RVQLLISYAR ANFPSTELLN YALQVEELTT AKKGNLILNV DGCIGILFID LMSSCGAFSK EEIDEVVRLG YLNGLFALGR SIGLIGHILD QKRLGSRLYR HPAEDIAYMM PSEEEIQCKR DR //