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Database: UniProt
Entry: A0A0W0GJT6_9CHLR
LinkDB: A0A0W0GJT6_9CHLR
Original site: A0A0W0GJT6_9CHLR 
ID   A0A0W0GJT6_9CHLR        Unreviewed;       712 AA.
AC   A0A0W0GJT6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:KTB48826.1};
GN   ORFNames=DEALK_16730 {ECO:0000313|EMBL:KTB48826.1};
OS   Dehalogenimonas alkenigignens.
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX   NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB48826.1, ECO:0000313|Proteomes:UP000053947};
RN   [1] {ECO:0000313|EMBL:KTB48826.1, ECO:0000313|Proteomes:UP000053947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP3-3 {ECO:0000313|EMBL:KTB48826.1,
RC   ECO:0000313|Proteomes:UP000053947};
RA   Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., da Costa M.S.,
RA   Rainey F.A., Moe W.M.;
RT   "Genome sequence of the organohalide-respiring Dehalogenimonas
RT   alkenigignens type strain (IP3-3T).";
RL   Submitted (JUN-2015) 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:KTB48826.1}.
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DR   EMBL; LFDV01000002; KTB48826.1; -; Genomic_DNA.
DR   RefSeq; WP_065128744.1; NZ_QEFQ01000001.1.
DR   AlphaFoldDB; A0A0W0GJT6; -.
DR   STRING; 1217799.DEALK_16730; -.
DR   PATRIC; fig|1217799.6.peg.1722; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000053947; Unassembled WGS sequence.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP 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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053947}.
FT   DOMAIN          18..113
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   712 AA;  75203 MW;  3A8839C85052136A CRC64;
     MDSNPVKASK PTNPLDGVFK PRSVAVIGAS RREGSIGHKI FTNLLDSSFR GPVIPVNPKA
     DAISGVKTYS SVLDIPEPVD LAVIVVPAET VLPMVEGCGR KGVKAVIVIS AGFAESGVEG
     IELQEKLTLI CRHYGMKLVG PNCMGVMNTD PSVNLNATFS HVFPPQGKIA MATDSGALGL
     VILEYASNLG IGLSNFASVG NRADVSSNDL LEYWRDDPGT SAIMLYLEAF GNPKNFIRLA
     RSISPNKPII ALKSGRSSAG SRAAASHTGA LATVDVAVDA LFAQGGILRV DNLERLFDVA
     DILSRQPIPR GSRVAVLTNG GGPGALTADA CAAAGLELPS LAEKTLQGLK ALLPARASLG
     NPIDITDVGA PEYQGALRLL AADNNIDAVI VIFIPPVFAC PEDVAAVIRE MEPEFRRRGK
     PLLASFMGKR GCVPGTIMPP GAAGVPSFSF PEAAVYALAR ARDYGLIRNQ PAGRLVNLPG
     IDRGKARRIV ESAGDGWLPA KSVFALLTAY GIKSMALRFA EDLDAAIGAA EDIGYPVALK
     LDSATIVHKT EVGGVALDIG SSEELRAAYH RMLGRLAAVG RAAEVRGVTV QKMAGEGVEL
     IAGITRDETF GPLILFGLGG IYTELFEDRT LRIQPLTDKD AQEMVRSVRA FKLLEGFRGE
     PPADVPAVEE LLLRLSAMAE DLPRIKELDL NPIRAFTAGK SYTVVDARIL IE
//
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