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Database: UniProt
Entry: A0A1H9VN89_9ACTN
LinkDB: A0A1H9VN89_9ACTN
Original site: A0A1H9VN89_9ACTN 
ID   A0A1H9VN89_9ACTN        Unreviewed;      1897 AA.
AC   A0A1H9VN89;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Ketoacyl-synthetase C-terminal extension {ECO:0000313|EMBL:SES22663.1};
GN   ORFNames=SAMN04487983_10372 {ECO:0000313|EMBL:SES22663.1};
OS   Streptomyces sp. yr375.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761906 {ECO:0000313|EMBL:SES22663.1, ECO:0000313|Proteomes:UP000198568};
RN   [1] {ECO:0000313|EMBL:SES22663.1, ECO:0000313|Proteomes:UP000198568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR375 {ECO:0000313|EMBL:SES22663.1,
RC   ECO:0000313|Proteomes:UP000198568};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR   EMBL; FOFF01000037; SES22663.1; -; Genomic_DNA.
DR   STRING; 1761906.SAMN04487983_10372; -.
DR   Proteomes; UP000198568; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0033068; P:macrolide biosynthetic process; IEA:UniProt.
DR   CDD; cd08952; KR_1_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 6.10.140.1830; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR041618; PKS_DE.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF18369; PKS_DE; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..459
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1537..1619
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          463..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1897 AA;  195963 MW;  8D530D027E757A4F CRC64;
     MSDVTRLRDY LRKVTVDLHE TRQRLREYEQ RDAEPVAVVG MACRFPGGIA SPDDLWEVVA
     AGHDVMSAFP GNRGWPLDRL YDPDPDRPGT TYVKEAGFLH DVADFDATFF GISPREALAM
     DPQQRLLLET SWEALEHAGI DPLSLRGSQT GVFVGSGAQD YGMLAAQAAD DLEGFLLTGN
     AISVLSGRVS YTLGLEGPAL SVDTACSASL VALHLACQSL ARGECSLALA GGASVLSTPA
     GFVELSRQRG LAPDGRAKAF AEAADGTAWS EGAGVLVVER LSDARRNGHR VLAVVRGSAV
     NQDGASNGLT APNGPSQERV IRAALADADL TAADIDAVEA HGTGTALGDP IEANALLATY
     GRNRPADRPL WLGSLKSNLG HSGAAAGVGG VIKMVMALRG DHLPRTLHVD APTSKVDFSA
     GNVALLTEPQ PWPQTGRPRR AGVSAFGISG TNAHVLLEQA PEFITPDPDT PDGRPTSPGT
     TAPAGTAVPS ARASTTAPAA TTAPAGATAS SAPADTTAPA GTTAPAGTTA PAGTTAPAGT
     TAPAGTTAPA GTAAPAATTA PAGTTVPTAP PAPVPIAVSG RSREALRAQG DRLLPLVQRG
     TPLPDLAAAL LRHRSALEHR AVVVADDADT VAAGLRALAE GRPHDAVVSG TAVPTDRVVF
     VFPGQGSQWA GMAVELLDSA PVFAAHLAEC DSAARAFVDW SIADVLRGAP GAPSMEPIEI
     LQPVLFAVMV SLAELWRSYG LTPAAVVGSS QGEIAAAYTA GALSLHDALK IVVLRSQLFA
     DELRGNGAVV SVAAPEQQVR ARLAAQGDDT LHIGGVNGPN AVTVVGPPAG LDRFVAEATA
     DGLRARLVGS TVASHCDQVD PLRERILDMF ADIRPTATTV PFCSTVTGEF TDPATLGAPY
     WFDNARRPVA FDPAVRTLLA AGLRFFVEVS PHPVLVTAVQ DIAEDAGADA AVVGSLRRDQ
     GGLDRFLRSV ADAHTRGAPV DLGVALAGRD TAWVDLPTYP FQRQRYWPEA DATAVSDPAA
     PADAVESGFW EAVENADLAG LTETLELDAE PLAAVLPALS AWRRQRREQS VVDSWRYALD
     WRPVPDPASP RLSGDWLVAV PPGHTGPEPD ALARHGARVI RVEVTADPSA PEALRTALAG
     ARPDGVLALL DWPAAVSLVR ALLELGVAAP LWFTTTEAVA LDAAPDGDPD RAALWGLAPT
     VSLEHPDLTG GIVDLPARPD ERALTRWCAA LSGRTGEEQL AVRPAGLFAR RLVRSPLTAP
     TGAAWRPTGT TLVTGADTAV GAAVARSLAA AGAPALLLTV DPGGDAPAED ATAELRELGV
     EVRTVACDLT DRAAVAALLA ELPAGQPLTA VVHTAVPLDE TPLSTLDGAA ASAPRRGVTA
     AWHLHELTRD APLTAFVLFS SISGTFGGIG QAAYAAATAG LDALAEHRAA AGLPALSVAW
     APWADPADTT GVAATRRERL ASRGIGVLDE HRALAALGDA LTAGDTRLLL AEVDWPRFRG
     AYTLTGPRPL IAEFTPDRGR RTATGPATPV VGELAALPAA ERLGVLLAAI TGQAAAVLGF
     PDSSAIDPAR RLLEHGFDSL TTLELRNRLT AATGVRLTAA TLFEHDTPEA LARHLQGELG
     PDPVATAVAE PGLFAAFQHR AAEAGKTGEF VELLAAAAKL RTTFGSAEEA GALPEPVELT
     AHDEGPVLVC LPTVLATSGP HQYARFAAGL RERRAVSAIA LPGYLDGEPL PADRPAAIEA
     ATRQVLAAAG ERPVVLVGYS SGGLLADGVA ARLAALGRPA AALVLIDTFV FGAELPTSGA
     ALFEQMFARL ADSGAATDAR LTAMGGYLRL LTDWEPGACP TPILVARATE PLAGFDRPPA
     TWAYPHDAVE LVGDHFTVLE EHADRTAQAV HEWLEKR
//
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