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Database: UniProt
Entry: K2CTA5_9BACT
LinkDB: K2CTA5_9BACT
Original site: K2CTA5_9BACT 
ID   K2CTA5_9BACT            Unreviewed;      1038 AA.
AC   K2CTA5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   28-JUN-2023, entry version 39.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:EKD77654.1};
GN   ORFNames=ACD_42C00245G0008 {ECO:0000313|EMBL:EKD77654.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD77654.1};
RN   [1] {ECO:0000313|EMBL:EKD77654.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD77654.1}.
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DR   EMBL; AMFJ01017516; EKD77654.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2CTA5; -.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EKD77654.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          528..605
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          616..1036
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   1038 AA;  115214 MW;  1C0A1C4D9E800501 CRC64;
     MRFEAKIIET AKQYPHAIAL TEWDGNQWQE KSYAALIQAA QQFSDQLNLY HIKKGERVIL
     ITHNRIQGVV ALLGIWLAKA TAVLIDPDLP ESACLQHCQI ADARFFIVEK EITQTVRESV
     NAKYLIEITD CDFIWHEKKV ELTETIYEDC SESIATLIFT SGTTGDYKSV ILTHANYLYL
     SQFYQHFSEQ DGCMLTVLPL FHVAGLFCGF LQPLCLGVNI VFFRAFSAES FQSAFSNYHP
     TILLSVPRLL EMIHQKIQLA LNEKGKIAQC IFKIFIHTAY FSYRYLHVNM GKIVFRKIHH
     QFGGCLKRIL CGSAQLSAHL QKQFLSLGFD LYCSYGLTET CGPITFTIYQ HRFRLGSVGR
     CDEINNLTIS TEGEVLYRGP ALMSGYFRDP IATAEVIRDG YFHTRDLGKL DRHNNLYIEG
     RLKEVIVFSD GKKAFPEQIE KQYALIPGIK EYAVFGVTER DATFAVLAFV PNQIAESLLI
     KSKLFQRASH LKSPFRITDV FFTEKIPRSS TLKVKRHLLA EHYLSGDASR DDLVEKISQC
     FKVILSDKKE WITPDITFAE LGIDSLLAAQ LCEIINAELH LSINPTEFWF SSTIRELALS
     VRADKKSVKN SVRHPNEKIA IVAQTGVFPG GAKNIDIFWK NLLSGNDAIV AIPASRWDVD
     TYYDEYALAP GKTNSRWGGF IDLPDYFPLS EFGLKPAATN EMDPRQKIVL LQVQSLLKNN
     AKTPKNTGFF IGAGFPDFMI HAVKTVPLTK MNPYSGMGIA DFSLASRVAY HFGFEGPAMV
     INTACSSALV AVHQAVRALQ HHDCDAAIAG GINVILEPDI SVLLTKGGFL SPEGRCKSFD
     ANANGYVRSE ACGLVLLKRY VDAKRDHDSI LAVIAGSAIN QDGASTGLTA PNGNAQIACY
     EAALARAEIQ ASEVDFIEAN GGATQLGDAI EMQSIQRVYD QQRNKNKPLL IGAVKSNIGN
     GESAAGIAAL IKTVCVLQHQ MVPPNLHYHH ANPNIDLQHS AVCLPTTVTR FQKPCLVAAV
     SAFGIAGTNV HIIMEVDT
//
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