ID   A0A1H5N7D0_9ACTN        Unreviewed;       745 AA.
AC   A0A1H5N7D0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SEE97360.1};
GN   ORFNames=SAMN05216533_4802 {ECO:0000313|EMBL:SEE97360.1};
OS   Streptomyces sp. Ag109_O5-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEE97360.1, ECO:0000313|Proteomes:UP000198812};
RN   [1] {ECO:0000313|EMBL:SEE97360.1, ECO:0000313|Proteomes:UP000198812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEE97360.1,
RC   ECO:0000313|Proteomes:UP000198812};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNTQ01000001; SEE97360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5N7D0; -.
DR   STRING; 1855349.SAMN05216533_4802; -.
DR   OrthoDB; 190266at2; -.
DR   Proteomes; UP000198812; Unassembled WGS sequence.
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:UP000198812}.
FT   DOMAIN          538..578
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   745 AA;  78831 MW;  301B2B92A77706C9 CRC64;
     MLGSTHGTLT TDSRRARVIA CGEQRPGPAV HGRAAEAGDA DVLDVSGRPL YADVPDLDRF
     FRPESVAVIG ASDAEGRPNT GITRQLLDWA GRVGARVHPV HPVRPSVFGI ACVASVADLP
     EQVDLAVLLV ADPLPVIEEL AEAKVRFAVA FASGFAETGE EGAAAQTRLA AAVRRSGLRL
     LGPNTNLNAF ERFRDDLEGP AIALITQSGH QGRPVFAAQE LGIRLSHWAP TGNEADLETA
     DFLSYFAERP EVGAIACYVE GLKDGRAFLL AADRAARRGV PVVAVKVGRT EAGARTAASH
     TGKLTGADDV VDAALRQYGV IRVDGLDELQ DTAALLARAR APRADGVVVY SISGGTGAHV
     ADLAAGLGLR LPVLSAARQA ELHQWIPEYL SVANPVDNGG HPVGDWRGRK IIDAILADPE
     VGVLVCPITG PFPPLSDRLV QDLVDAAEAT DKLVCVVWGS PVGTEAAYRE VLLGSSRVAT
     FRTVGNCLTA VRAHLDHHRF VSDYRSPFDE APRTPSPSYR KALALMRPGQ QLSEHAAKQL
     LRAYGIRVPR EQLVTSAAAA VRAAGLVGYP VVMKASGGQI AHKTDLGLVK IGLTSASQVR
     DAYRDLTDIA RYEGVALDGV LVCQMVERGV EMVVGVTHDD LFGPTVTVGL GGVLVEVLHD
     AAVRVPPFGE DQARDMLAEL RGRALLDGVR GRPPADLDAL VEVILRVQRM ALELGDQLAE
     LDINPLMVLE QGQGAVALDA LAVCR
//