ID   A0A257L9X5_9BACT        Unreviewed;       684 AA.
AC   A0A257L9X5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   22-FEB-2023, entry version 7.
DE   SubName: Full=CoA ligase {ECO:0000313|EMBL:OYU96416.1};
GN   ORFNames=CFE21_08450 {ECO:0000313|EMBL:OYU96416.1};
OS   Bacteroidetes bacterium B1(2017).
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=2015582 {ECO:0000313|EMBL:OYU96416.1, ECO:0000313|Proteomes:UP000216329};
RN   [1] {ECO:0000313|EMBL:OYU96416.1, ECO:0000313|Proteomes:UP000216329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:OYU96416.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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:OYU96416.1}.
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DR   EMBL; NKJG01000002; OYU96416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257L9X5; -.
DR   Proteomes; UP000216329; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:OYU96416.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216329}.
FT   DOMAIN          6..100
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   684 AA;  73182 MW;  BA15D013B03CAEE8 CRC64;
     MINKQLISPE SIVVVGASED IEKPGGKVLL NLLNGGFTGK LYGVNRKGKS IEGVNTVRSI
     DELPSIDLAI ISIPAETCLE AVKGLIEKGA KAFIIFSSGF GEAGPIGKER EKELVAMINQ
     ANACLIGPNC VGVINQNYKG VFTSPIPEYH ADGCELISSS GATAVFIMEA ALSTGLRFSS
     VYSIGNAAQT GVEEVLEYLD KNYEEGKSAK VKLLYLESIK NPFKFLKHAS SLIKKGCKLA
     AIKSGHSEAG SRAATSHTGA MASSDTVIRA LFKKAGIVYC SGRAELISVG CIFQSKTLNG
     KNIAIVTHAG GSAVMLTDAL SSRGLQVPAI HGPEADMLLT KLNPGSTVGN PIDFLATGNA
     EQLGLIIDFC EGLSEIDAII VVFGSPGLFN VKQVYNVLNQ KMNACSKPIY PVLPSLVNAK
     EEIEGFLAKG NINFPDEVVL GSALPHVYHC APPSFELTRL ARMEDATIRG IINQATDGYL
     SPETARELAL AAGINMAKEF VCITLEDLLK AKEQMMFPLA MKVIGPIHKT EVNGVSLHIN
     SWEKLVSEYN RMLKIPDSRG VVVQEMVEGE ELFVGASREG DFGHLIVCGL GGIHVEVLKD
     LAFGLAPLGK EEALDMVNSL KGYPILAGYR NRKGIDIDKF VDAIVRVASL VHLAPEISEL
     DINPFKAGPD YLKAVDVRIR ITKK
//