ID   K7WVQ9_9NOST            Unreviewed;       922 AA.
AC   K7WVQ9;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:AFW94646.1};
GN   ORFNames=ANA_C11891 {ECO:0000313|EMBL:AFW94646.1};
OS   Anabaena sp. 90.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW94646.1, ECO:0000313|Proteomes:UP000010101};
RN   [1] {ECO:0000313|EMBL:AFW94646.1, ECO:0000313|Proteomes:UP000010101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90 {ECO:0000313|EMBL:AFW94646.1};
RX   PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA   Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA   Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT   "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT   cyanobacterium Anabaena sp. strain 90.";
RL   BMC Genomics 13:613-613(2012).
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DR   EMBL; CP003284; AFW94646.1; -; Genomic_DNA.
DR   RefSeq; WP_015079807.1; NC_019427.1.
DR   AlphaFoldDB; K7WVQ9; -.
DR   STRING; 46234.ANA_C11891; -.
DR   KEGG; anb:ANA_C11891; -.
DR   PATRIC; fig|46234.3.peg.2110; -.
DR   eggNOG; COG0045; Bacteria.
DR   eggNOG; COG1042; Bacteria.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_007415_0_2_3; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000010101; Chromosome chANA01.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.630.30; -; 1.
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; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000182; GNAT_dom.
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; PF13302; Acetyltransf_3; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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.
DR   PROSITE; PS51186; GNAT; 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:UP000010101}.
FT   DOMAIN          517..553
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          763..922
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   922 AA;  100102 MW;  E48D57C8162F2102 CRC64;
     MEAPIKPITN KPYNIFCPEK LNPLDAIFAP KTVAVIGASE KPGSVGRNLL WNLITNPFGG
     TVFPINPQHS SILGIKAYST IFDVPEKIDL AVIATPASTV PKIIADGVES GIKGAIIISA
     GFKEAGEKGI ALEQEILQQA HRGKIKIIGP NCLGLMNPIS GLNATFASKM ARPGNVGFIS
     QSGALCTAIL DWSFQENVGF STFISIGSML DISWGDLIYY LGDDPHTKSI VIYMESIGNA
     RSFLSAAREV ALTKPIIVIK AGRTPAAAKA AASHTGSLAG SDAVLDAAFR RCGVLRVNSI
     SDLFDMSEVL AKQPRPQGPR LTILTNAGGP GVLATDTLIE SGGELAAISP EIMSSLNEIL
     PPQWSHNNPI DILGDADPQR YKKALEIITK DPNSDGLLVI LTPQAMTDPT QIAEQLKPYV
     QMSGKPILAS WMGGADVAAG QQILNSQGIP TYSYPDTAAR VFSYMWKSSY NLRGIYETPV
     LPTLTCDANT RNCAKVENII QAAKTAGRTI LTEFESKEIL AAYGIPIVAG CIAESADKAV
     ECAENLGYPV VLKLYSQTIT HKTDVGGVQL NLQNAESVKL AYQNIETSVK QKAKAADFLG
     VTVQPMIKTD GYELIIGSSL DPQFGPVLLF GAGGQLVEVF QDSSIALPPL NTTLARRMME
     QTKIYKALQG VRGRKSIDIA ALEQLMVEFS QLVVEQPGIK EIDINPLLAI PPTPIHPGGL
     IALDARVVLH SADVEKHQLP KLAIRPYPSQ YISNWKLNNG TPITIRPIRP EDEPLMVEFH
     KTLSEESVYF RYFHMIKLSQ RITHERLTRI CFIDYDREMA LVAEYQNPET EKREILAVGR
     LSKLHGSNAA EFAMLVSDKF QDQGLGTELL RRLLEVGKNE RSCCIYADIL ADNSGMQRVC
     EKLGFQITNT SDTTVLRAEI KL
//