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Database: UniProt
Entry: A0A1F6M216_9BACT
LinkDB: A0A1F6M216_9BACT
Original site: A0A1F6M216_9BACT 
ID   A0A1F6M216_9BACT        Unreviewed;       380 AA.
AC   A0A1F6M216;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGH65667.1};
GN   ORFNames=A3J66_01305 {ECO:0000313|EMBL:OGH65667.1};
OS   Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_02_FULL_47_14.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1798680 {ECO:0000313|EMBL:OGH65667.1, ECO:0000313|Proteomes:UP000176282};
RN   [1] {ECO:0000313|EMBL:OGH65667.1, ECO:0000313|Proteomes:UP000176282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGH65667.1}.
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DR   EMBL; MFQB01000046; OGH65667.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6M216; -.
DR   STRING; 1798680.A3J66_01305; -.
DR   Proteomes; UP000176282; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR032263; Citrate-bd.
DR   InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF16114; Citrate_bind; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..143
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          239..370
FT                   /note="ATP-citrate synthase citrate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16114"
SQ   SEQUENCE   380 AA;  42795 MW;  CC6C992F3BD8E56E CRC64;
     MNLYEFEGKK IFETYGIQVP RGVVVRRGEN YGDAYQQLDV KEVVVKAQTL SGKRGKSGGI
     TFASSKEETE VCCEKLFNTD IRGQYIAAIR IEEKLVIAEE HYLSITYDTN KRRPVLIYSA
     QGGMDIEDVP EEKIVKQWID IRSESVGSDI PFANELWQVF LKEDTRLVEI NPLVKTVDGV
     WIAADAKIAI DDDAFFRHEE WKTFEPRSMM GRLPTERENQ AKKIDEGEAY YRGTAGKYIE
     MDGDIALILN GGGASIANMD ALIQLGLKPA NYTEYSGNPP REKVRALTEV VLSKPGIRGL
     WMCGVVANFT NMKETFLGVI DVLDELKPTY PIVVRRDGPE SAEAIRLVRE CAARNHLNLK
     IFNKDVSMTE SAHVLANMVR
//
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