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Database: UniProt/TrEMBL
Entry: R4KHK5_9FIRM
LinkDB: R4KHK5_9FIRM
Original site: R4KHK5_9FIRM 
ID   R4KHK5_9FIRM            Unreviewed;       715 AA.
AC   R4KHK5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=ADP-forming acetyl coenzyme A synthetase {ECO:0000313|EMBL:AGL02698.1};
GN   ORFNames=Desgi_3353 {ECO:0000313|EMBL:AGL02698.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL02698.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGL02698.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL02698.1,
RC   ECO:0000313|Proteomes:UP000013520};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA   Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA   Brambilla E., Spring S., Stams A.F., Woyke T.;
RT   "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003273; AGL02698.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4KHK5; -.
DR   STRING; 767817.Desgi_3353; -.
DR   KEGG; dgi:Desgi_3353; -.
DR   eggNOG; COG0045; Bacteria.
DR   eggNOG; COG1042; Bacteria.
DR   HOGENOM; CLU_007415_3_1_9; -.
DR   Proteomes; UP000013520; Chromosome.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013520}.
FT   DOMAIN          508..544
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   715 AA;  76477 MW;  E25DCA205EF395E7 CRC64;
     MLRQLSTRHI GEVRIVIDLT SMSRPQSVAV VGASPKPGKI GHTILGNVIS SGYKGKIFPI
     NPKEKEIAGY KTYTAVSEVP EPVDLAVIAV PAARVLDVVR DCGQAGVKSL VVITAGFKEV
     GAQGLEMEKQ LVESCRKYGM RLLGPNVVGI IDTHTPINAS FSATFPQQGE IAFLSQSGAM
     LVAILDWSAS IGIGFSKVVS LGNKADLSEI EFIEDAAADP HTKVILCYIE DIVDGPRFLD
     VASRASRKKP VIVIKSGTSQ AGAKAASSHT GALAGSDLAY DVAFRQCGIL RARTMTELFD
     LAVAFAKAPV PKGNRVAIVT NSGGPGIIAT DNVEAKGLQM ASFDKATIEE LRANLPAEAN
     IYNPVDVLGD AKADRYKFAL QKVCADPNVD SVVVLMCPVG VTEPIETTEA LLEMRQSFPE
     KPIFAAYMGG ETLAGGAAML AKAGVPCFTF PEPAIASISG LVRYNEVLDV PKGNGNQDLA
     NIDRKGVKAI FYDVIKDNRL VLLGSEATEI AKCYGIPAAP VVLATSPDEA AAEADKMGYP
     VVLKVASPKI LHKTDVGGVH IGLNTAEEVR HAFVEIMENV HGYMPQAVIY GVEVQKMMPK
     GTELIIGMTR DIQFGPLIAF GLGGIYVNLI KDVSFRLARG LTAREIEHML RETKAYTLLR
     GYRGEKPRDI EALADTIRRV AELVNDFPEI SEMDINPVFA YENGLSALDI KITIS
//
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