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Database: UniProt
Entry: D5E7L2_METMS
LinkDB: D5E7L2_METMS
Original site: D5E7L2_METMS 
ID   D5E7L2_METMS            Unreviewed;       697 AA.
AC   D5E7L2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE            EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN   OrderedLocusNames=Mmah_1654 {ECO:0000313|EMBL:ADE37150.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE37150.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE37150.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP001994; ADE37150.1; -; Genomic_DNA.
DR   RefSeq; WP_013038092.1; NC_014002.1.
DR   AlphaFoldDB; D5E7L2; -.
DR   STRING; 547558.Mmah_1654; -.
DR   GeneID; 8983834; -.
DR   KEGG; mmh:Mmah_1654; -.
DR   HOGENOM; CLU_007415_3_1_2; -.
DR   OrthoDB; 18103at2157; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; 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; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR014089; AcCoA-synth-alpha.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR043938; Ligase_CoA_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   NCBIfam; TIGR02717; AcCoA-syn-alpha; 1.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF19045; Ligase_CoA_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          486..522
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   697 AA;  75031 MW;  8EF63493B116739E CRC64;
     MLSSLFNPKS VAVIGASNKK GKVGNAVLSN LIKDFGGNIY PVNPRNEEIE GLECYASIND
     VSDDVDLAVV VIPAKIVPST LEECGRAGVK YVVVISAGFK EAGVEGAKLE RSALEICRKH
     DMRMVGPNCL GIMDPVAGLN ASFAASMAYE GNIAMMSQSG AICTSTLDWA EANGMGFSKF
     VSLGNKADLG ENQFLAEFRD DPSTSVIAAY LEGIKNGSQF IEIARDVSRK KPVVLVKSGR
     TAAGSRAVSS HTGTLAGSDQ AYNAAFDKAG VVRADTLEDM LDYIRAFSTQ PIPAGRRIAI
     LTNAGGLGIL TADACYYEGL ELASFSAETI EGLREFLPDA ASFYNPVDVL GDASAKLYGD
     ALEIVLKDPN VDGVILLTSP QAMTDVTSIA RIVIQKVEYS DKPVLCSFVG GTRVMEGNFI
     LVAGGVPNYI FPERAVASMG ALCDYGKRRN MIFPLPEPVH SDRKMASALL GKAAAKDKKT
     LGLESFDLLK AYGIPVVEIG KASSVEEAIE ESERIGYPVV MKVLSPDISH KTDVGGIRLS
     LMNKEDVRRA YHTMMSDVRR YMPSARIAGV QLQRMIEGGR EVIIGMNRDV QFGPLLMFGL
     GGTYVEILKD VSFRLAPLNE KDAHSMISSI RSYPLLTGVR GEKAYDVDAV ADVLIRVSRL
     VEDFPQILEF EINPLMVLPE GDGCFAMDMR LTLKESN
//
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