ID B9M8K3_GEODF Unreviewed; 695 AA.
AC B9M8K3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Acyl-CoA synthetase, ADP-forming {ECO:0000313|EMBL:ACM18538.1};
GN OrderedLocusNames=Geob_0165 {ECO:0000313|EMBL:ACM18538.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM18538.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM18538.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001390; ACM18538.1; -; Genomic_DNA.
DR RefSeq; WP_012645267.1; NC_011979.1.
DR AlphaFoldDB; B9M8K3; -.
DR STRING; 316067.Geob_0165; -.
DR KEGG; geo:Geob_0165; -.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_3_1_7; -.
DR OrthoDB; 9791027at2; -.
DR Proteomes; UP000007721; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
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; 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:UP000007721}.
FT DOMAIN 494..530
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 695 AA; 74541 MW; E0123B7570F3D8AA CRC64;
MLDSLFKPRA VAIVGASTKE LSIGNVIIRN LQKYGYKGEI YPLNPTAPEV CGIKAYKTLE
EIPGEVDLAH VIIPSKFVPQ TIEDCGRKGI KAVIINSAGF SELGEEGARL QEDFLRRGKE
YGVRVFGPNC QGIINSDPEL KAYCNFTFTY PEPGYVSVVA LSGGVGALIM QALADLGVGQ
RLYASNGNAC DISIPEIVRY YGADEGTKAV ILYTEGFSDP KAFLEAAHQV TAKKPILAMK
AGRTEQGAKA ASSHTGSLAG VDIATELIFE KTGILSFTDE GEMARAAMAF ATQPIPKGNR
VGIITNTGGP AVIATDVLVS CGLDVPKLSE RSIERLKESQ FPEAALENPI DVVATAGGPQ
FRGALDVLLH EEGVDSIFIN FVTAPFTDTH EVARQIVEVS RLGKKPIVCN FMTDLSQERY
QITRDILKKG GVPFYANPSD AAKAMGALTR YGRLKQRDIG KPQTFANVDA AKARAIVEEA
RQAGRSVLSA TDVYTIFEAY GIPVAGWGVT VNTAEAVAAA DRIGYPVVVK VDCEAIDHKS
DMGGVAVNLK DAASVQATVE DMQRRLGHFG TLKFFVQKFL PGGRELIIGA TAERGLGHLV
MFGLGGIYVE VLKDVSFKIA PVTQVEAEEM LSSLRTAALL NGVRGEKGIN REAVMNIIQR
ASQLLGDLPM IQEMDMNPLM AFADGAFAVD GRIRI
//
