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Database: UniProt
Entry: K9WHU0_9CYAN
LinkDB: K9WHU0_9CYAN
Original site: K9WHU0_9CYAN 
ID   K9WHU0_9CYAN            Unreviewed;       918 AA.
AC   K9WHU0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:AFZ19980.1};
GN   ORFNames=Mic7113_4281 {ECO:0000313|EMBL:AFZ19980.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ19980.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ19980.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ19980.1,
RC   ECO:0000313|Proteomes:UP000010471};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003630; AFZ19980.1; -; Genomic_DNA.
DR   RefSeq; WP_015184116.1; NC_019738.1.
DR   AlphaFoldDB; K9WHU0; -.
DR   STRING; 1173027.Mic7113_4281; -.
DR   KEGG; mic:Mic7113_4281; -.
DR   PATRIC; fig|1173027.3.peg.4731; -.
DR   eggNOG; COG0045; Bacteria.
DR   eggNOG; COG1042; Bacteria.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_007415_0_2_3; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000010471; Chromosome.
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:UP000010471}.
FT   DOMAIN          518..554
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          758..918
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   918 AA;  100261 MW;  9AB3F3A5C4382B5C CRC64;
     MSKTLMQTTD PAHDVLRYER QPLDAIFAPK NVAVIGATEK AGSVGRTLLW NLISNPFGGT
     VFPVNPKRPS VLGIKAYPSI AAVPETVDLA VVVTPAPTVP GVIGECVAAG VKGAIIISAG
     FREVGEQGIQ LEQDVLKQAR QGRMRIIGPN CLGVMSPVSG LNATFASAMA RPGNVGFISQ
     SGALCTSILD WSFRENVGFS AFMSIGSMLD VNWGDLIYYL GDDPATHSIV IYMESIGNAR
     SFLSAAREVA LTKPIIVIKA GRTEAAAAAA ASHTGALTGS DEVLEAAFRR CGVLRVNMID
     DLFNMAEVLA KAPRPKGKRL TIITNAGGPG VLATDALISE GGELAPLSPQ TMEELNQLLP
     THWSHSNPID VLGDADPNRY AKACEIALKN PESDGLLAIL TPQAMTDPIQ TAKQFVERLQ
     GSTLPAKPIL ASWMGGAEVA GGEAMLNEAR IFTLPFPDTA ARVFNYMWRY AYNLRGIYET
     PVLEGGADEK APDRVRATEI IQSIRASGRT LLSEFESKQL LKAYGIPTVE THIAQSEAEA
     VQLAQEMGYP VVLKLYSETI THKTDVGGVK LNLADADDVR KAYQAIESAV LLKAGAEHFL
     GVTVQRMLKL DGYELILGSS PDPQFGPVLL FGTGGQLVEV FKDRALGLPP LNTTLARRMM
     EQTKIYTALK GVRGRAPVDL AMLEQLLIQF SQLVVEQRWI KEIDINPLLA SADGLMALDA
     RVVLHSLDVP EDKLPQAAIR PYPIQYVSDW TMKNGTSIKI RPIRPEDEPL VVKFHENLSE
     ESIYSRYFHL MKLQTRVAHD RLSRICFIDY DRELALVADY KDPATGEHHL LGFGRLSKLH
     GRDEAEFSML IGDRFQCKGL GTEFLRRLIE IAKDEQLQYI TAEILSENRA MQHVCQKLGF
     RLEPTSEPSI MKVVYELR
//
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