ID A0A0Q1C2E0_9BACT Unreviewed; 430 AA.
AC A0A0Q1C2E0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=ATPase {ECO:0000313|EMBL:KQC08656.1};
GN ORFNames=APR54_04355 {ECO:0000313|EMBL:KQC08656.1};
OS Candidatus Cloacimonas sp. SDB.
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=1732214 {ECO:0000313|EMBL:KQC08656.1, ECO:0000313|Proteomes:UP000052007};
RN [1] {ECO:0000313|EMBL:KQC08656.1, ECO:0000313|Proteomes:UP000052007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC08656.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000256|ARBA:ARBA00009182}.
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:KQC08656.1}.
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DR EMBL; LKUH01000248; KQC08656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q1C2E0; -.
DR Proteomes; UP000052007; Unassembled WGS sequence.
DR GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.30.470.110; -; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR032263; Citrate-bd.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR23118:SF58; ATP CITRATE SYNTHASE; 1.
DR PANTHER; PTHR23118; ATP-CITRATE SYNTHASE; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF16114; Citrate_bind; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 43..208
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 249..425
FT /note="ATP-citrate synthase citrate-binding"
FT /evidence="ECO:0000259|Pfam:PF16114"
SQ SEQUENCE 430 AA; 48293 MW; 583B69367C7C4CC5 CRC64;
MAQKGIREYD AKRMMSKALP HFSDGKIKFE ASQVLIGPKT DLSKIAEDHP WLKTEKLVAK
PDQLFGKRGK NNLLYVNKSW SEVKNWISER MNKTVTISQT TGETTGILNY FLVEKFVPHE
EEYYIAITTH REYDTIHFSL KGGVNIEEVW DSVVTLDIPI LKKIDEFDIA GFLPQELGGK
KKIIAEFTKA LYKMLVEYHF VYLELNPFTF VDGAPVALDA VAKVDDYASY QCAEYWGNLK
FPNPFGLEKT PEEEKVDDLD DRTGASLKLT ILNPDGRIWN LVAGGGASVI YADTVVDLGY
TSELANYGEY SGNPSTELTY AYTKTILDLM TRKKDAQGRP KFLLIGGGIA NFTDVAKTFT
GIIQAIKEYK DKLKAANVNI YVRRGGPNYM EGLNNMKEVG IKLGIPIEVY GPETHMTKIV
SMALDKKVGE
//
