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
//