ID A0A0K9XAK5_9ACTN Unreviewed; 2503 AA.
AC A0A0K9XAK5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNB50454.1};
GN ORFNames=AC230_20975 {ECO:0000313|EMBL:KNB50454.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB50454.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
RL Submitted (JUL-2015) 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:KNB50454.1}.
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DR EMBL; LFXA01000014; KNB50454.1; -; Genomic_DNA.
DR RefSeq; WP_049717850.1; NZ_LFXA01000014.1.
DR STRING; 1678637.AC230_20975; -.
DR PATRIC; fig|1678637.3.peg.4493; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000037288; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037288};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..431
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2412..2490
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 41..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2503 AA; 263574 MW; 23DA7CF4AF906103 CRC64;
MESCGSSVPV AVVGVACRLP GGITQLDGLW RALADGRDLI SPGPPDGRFD AARFSDPDPE
RPGRAYTMAG GYLEDVAGFD PEYFGISPRE ARHMDPQQRM LLEMTAEALD DAAIAPAALA
GSDTAVYVGV SDLSYGGLQM SKVEEICGHS MSGSALSITA NRLSYAFDLR GPSLAVDTAC
SSSLTAVHQA CEALRTGRSP VAVAGGANLL LSPAHFIGFS KAMMLSPRGR VAAFSAGADG
YVRAEGGGVV VLKRLSDALA DGDRVHAVIA ASASNSDGRT SAMTVPSTEM QRRLLREAYE
RAGAAPDQVL YFEAHGTGTP VGDPLECRAV GEALGVRRTT GPLPIGSVKT NLGHMEPASG
MAGLFKGLLV LRHRTVPPSL HGDPPNPAID FTGLNLSPVH DACPLAGRED GVVGVNSFGF
GGANAHVVLS PPPARARTEL PPEHGPLPLV VSARTHDALA QAARAVAGRV REATPGDFYD
LCWTASRRRG RHPHRVAVLA SGPDEAAGRL EALAADGAGL AAAEVRVPEP GGTVFVYCGN
GTQWPGMGAA LMAGEPAFRA AVEAADAELE PLLGWSVARL LAGTHGTADG TADTATDAMT
EAMTDTARAQ PALFAYQLGL TALLAEHGVR PAAVLGHSVG EVAAAHACGA LGTAEAARVV
AARSRTQAAT AGTGRMAAIG LGEPDAREAL AAHGGRLEIA AVNSARDVTV SGDPAALDAL
GRELAARGVP FRALAVDHGF HSAAMDVIEE PLRAALAGLT SHAPRLPMYS TVTGDPVGAG
ELDAAYWWHN ARRPVRFADA VRRAAGAGLG AVVEIAPQPA LAGALCRIAA DAPRGAFPVV
SPVSRERCAG ADVRRAAARL LAAAEPAALD ARFPRPGAVA DLPPYPWQRQ RHWHGTPEHW
IRTSGDGVLV HPLLGERVPV LEPTWHTAVE RTRTPWLADH RIAGAVVMPA AGFVELALAA
AREVHSAGTP AEIDDLDIVR ALPLPWDAVT DVGLQTSLCD EDGILRVASR IGEPGGWRPH
ARARVRRLAA ARPDGMDTDA VRARLGRALD TGELYAGLAE AGLEYGPAFR VLRDLRASAG
EVLAGYRCDP PDDGYGGYVV HPALLDGALQ AGAPLLEVAE DGYLPARIDR VRFWAPPAPD
GLVHVRQRSR TAREAVWDVT VAGPDGTVAL ELTGCRLRRV GLRAGGRAEE YASVLRAAPL
AGQPVPPWTP PAPSEVAAAA AEGVRRVWES APVVGQFATG APMFRRMTAE CAVRAFARLL
PGRGTFTFDD LTAAGVLPRH GKLVRLLARL ARDEGLLADE GAGWRRLPAA DAPERPRGWE
FLSTLASWVA TGCLGQRFAL HLPDLLCGRR DPLDLLFQDS GPELAQLYYD LDPPTALHNR
LAAELLAAVV RSWPPDRPLR VLEIGAGTGG LTAHLLPLLD DRARYVFTDV SAAFFPAAQA
RFDAPAAHLS YRTLDLDRDA ADQGFDDGSF DVVVAGFALH TAADLRRSLG RLARLTAPGG
YLLALETHEP ELLALLFGAM ESFWSAQDRE LRPDSVLLPH DRWPGVLADG GFEDVVQTDV
PGMREQFSVL LARTPAGPPP ECPGPAPSED RSWLLVAEHE EEHALAGLLA ARLAAAGGSL
PEVRPWPAGP GEWEKALADD PDATVVLMLG AACDRAAGED PAAAVELAVR RAAALRSLAR
AEQGRTGDRA RRLVLVTHPS GALPAPERPA FPGQAAAWAV TRTLSREQDV TGRRISLDRG
PDPALDAARL ARELLADAPA EEGEQVHDEV ALTGGGRFVH LVERARPATV LARPDDGTAY
RLDLRDQGLA HRLRWTETEP PVPGPGEVVV AVRAAALNYR DVMVATGLLP PGAEDGLPSE
AFLGLEGAGV VTAVGEGVGR FDVGDRVFGF LPGAFASHVR VPATAVRRIP GGLSFADAAT
VPVAYFTVHH ALAHLARLRS GETLLVHGVA GGVGMAAGRF ALRAGARVIG TAGTPAKRDM
ATVFGAELVL DSRTPAFADA VLAHTGGRGV DVVLNSLSGD AGARTREVLA PRGRFVELGK
RDVFTNQRML QRPLAENASL FFVDAANLVW QDPRHAGTVF DEVAERLRTR TYLPLFHQIY
PAHRIDEAFR LMQHSKHLGK IVIGFDGPVP VHRAPRRLHL DGDGTYLVTG GLGGFGAETA
RRLAERGARH LALVSRRGPE APDAARLVGE LGALGARARA HAADVSDPAA VRALVEEVTA
AGRPVRGIVH AAMHLDDGAL AELDDDRFRS VLAPKWGGAL ALDALCPDAE FIAYSSVSPL
VGNPLQSNYA AANLAMEALV RARRAAGRPG LAVAWGAIGR VGYVARNNLT ASTTAVGCPP
MDPREALTAL EDLCERRAER TTFGRIDWQR LSVLLAPGAV PRFAAVLPDR IEGSDWQLDE
FLERLATATP AEAAGLLEDL VAGMAASVLH MAPGELDRHR PLQQYGMDSL MGLEMLSTFR
SRLQQDVPVM ELLHSDGSVH GIAGTVLPHL LRQARARVQD GGR
//
