ID A0A094RIK8_9ACTN Unreviewed; 724 AA.
AC A0A094RIK8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE SubName: Full=Putative acyl-CoA synthetase {ECO:0000313|EMBL:KGA04563.1};
GN ORFNames=GM46_12290 {ECO:0000313|EMBL:KGA04563.1};
OS actinobacterium acAcidi.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA04563.1, ECO:0000313|Proteomes:UP000029305};
RN [1] {ECO:0000313|EMBL:KGA04563.1, ECO:0000313|Proteomes:UP000029305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KGA04563.1}.
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DR EMBL; JNSG01000119; KGA04563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094RIK8; -.
DR Proteomes; UP000029305; Unassembled WGS sequence.
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; 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 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}.
FT DOMAIN 17..231
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 724 AA; 76868 MW; 7104D571991FB2FE CRC64;
MLVFVPSTET LSEEASKRLL SPFGLPFAVE RIALTIDDAC AAANSIGYPV VVKVSGDTIA
HKTERGLVRL RLADEEAVRN ACTDLLGRVT AADGQVSFLV AQMVSGNREF IAGVITDPQF
GRMAVLGVGG VLAEAIDDVA LSPLPLKERD ALSMMKSLRH QKMLGEFRGE AALDARSVLS
VLNGLSAACD ANPDIYSIDI NPLIVNASGE LVAVDALVEF NKVRSSTKSF EDQHPVARSN
RHFDALFNPN GVVIVGASSH PGKFGFVSLH NLLANEYKGS IFATNLQGEE VLGVQTLKSL
DDLPTGSADL AFFCTPAAAN EDLLRQCSEK GITSVFISSA GYRESGEAGE HAEQGLVSLA
NSLDILIAGP NGQGVVSTPR SLCCQIVAPY PPSGGISVAS QSGNFVSSFL NYSRQTGVGI
ARAVSAGNAA QVRVEDYLDW YTTDDSTRVG LAYIEHVSNG DRLKSAMTKM SERKPLVVVK
GGATTAGSKA ASSHTGALAS DDKVFDGVCR ATGAIRVDDI ERAFDVAASF STQPLPRGNR
VVVLTTVGGW GVVTADAIAR DGVLDLVDLP DDLMAQLGDL LPPRWSRNNP IDCAGGETRD
TIPQIMDIVT GHDQVDAVIF LGIGIQSNQA RLMREGSFYP DFGLERIVQY HNRQDERYAI
AAHEASQKYL KPVLIATELA VADPSNPGPA TVRDTGRLCY ASGSRAAYAL AQMVKYSNYR
ASVS
//
