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
//