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Database: UniProt
Entry: A0A1V2QXF6_9PSEU
LinkDB: A0A1V2QXF6_9PSEU
Original site: A0A1V2QXF6_9PSEU 
ID   A0A1V2QXF6_9PSEU        Unreviewed;      1686 AA.
AC   A0A1V2QXF6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ONI92818.1};
GN   ORFNames=ALI22I_01680 {ECO:0000313|EMBL:ONI92818.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI92818.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI92818.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI92818.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:ONI92818.1}.
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DR   EMBL; MTQP01000026; ONI92818.1; -; Genomic_DNA.
DR   RefSeq; WP_077003802.1; NZ_MTQP01000026.1.
DR   STRING; 1933778.ALI22I_01680; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000188617; 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; cd08956; KR_3_FAS_SDR_x; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR036299; Polyketide_synth_docking_sf.
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: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; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF101173; Docking domain B of the erythromycin polyketide synthase (DEBS); 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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
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:UP000188617};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..457
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1528..1603
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1686 AA;  177171 MW;  5BAFEE8085B070C7 CRC64;
     MADEDKLRDY LKRAIADARD ARRRLKEVEE REQEPVAIVS MACRYPGGVR SPEDLWRLVA
     DGVDAVSDFP DNRGWPDELY DVDPDRVGKS YSRRGGFLHD ADRFDPEFFG MSPREALAVD
     PQQRLLMETA WEAFERAGVD PHAVRGSRTG LFTGVMYNDY GSRADLPGRD FEGYLFSGSA
     GSIASGRVAY TFGLEGPAVT VDTACSSSLV AMHLAVNALQ RGECDLALAG GVTVMSTPVA
     FIEFSRLRGL APDGRCKSFG ASADGTGWAE GVGLLLLERL SDARRRGHRV LAVVRGSAVN
     QDGASNGLTA PNGPAQERVI RHALERARLS TSDVDVVEAH GTGTMLGDPI EANALLATYG
     QDRVGEPLWL GSLKSNIGHA QAAAGVGGVI KMVQAMRHGV LPRTLHAETP SPHVDWSAGA
     VSLLTQARPW PAVDRPRRAA VSSFGFGGTN AHVIIEQAPA PAVASVSAEV VGSPRSGAVP
     WVLSAASASA LREQAARLVD VAGEPVDVGF SLATGRAALE HRAVVVGNDR SSLLRGVAAV
     AAGDSAADVV FGTRRGGKTA LLFTGQGSQR VGMGLALARE FPVFAEAFDE VCSRFSLDRP
     LRSVIESGED LDLTGYAQPA LFALEVALFR LLESWGVRPD VVVGHSIGEL AAAHVAGVFS
     LEDACRVVEA RGRLMQALPV GGAMIAVQAS EDEVLPLLKG QSRLALAAVN GPRAVVISGD
     ARAAEAVAAQ LAAMGRKTKR LTVSHAFHSP HMEPMLEAFR AVVLGAGLGS ARIPYVSTVG
     EAESWESADY WVEQVRRPVR FHDAAARLVD QGVTTTLELG PDAVLTALVP EGVTAVPLLR
     AARPEPTTAV LALGQLHAVG VGVDWSGFFG EARFVDLPTY AFQRQRYWLN PTNADSGHPL
     LGEPVAVAGT GEVLFTSRVT ADRLPWVPEP FGTPVLPGAG FVEMALRAGD ELGTPAVAEL
     TVHAPVVLSG AVHLQLRAGA VDGGWRAVTI HARADDQADW KLHASGTLTA EERAAEPVDG
     TRDEYAVEPE EASRYSLHPA LSALAVHEGD RLAHVWRDVR LHAGGAAAVW VGATSGTGVE
     LVDAAGLPVL SVGAVELRAV EPAEVSASLP LHETRWVALP ADSGEHAVTW ASAEDPAHPG
     AQAVFADFRA TTGDVVASVH ARAGAALDLV QRWLAQDHQG KLVVLTRVDD LAGAAVTGLL
     RSVRSENPGR VFTVALDGDD IPFDVLARLV VTDEPEAEVR DGVAYVPKLE RVTGPERGLP
     EWGVPEWGVP EWGGTVLITG TGALAAAVAR HLVTAHGVTD LLLVSRRGER APGAAELKAR
     LTGLGATVRI EACDVADRDA LAATIAGVPL TAVVHTAGVL DNGLAPTLTA DRLADVLRPK
     VDGAWHLHEL ARDVKAFVLF SSVVGIFGGP GQANYAAANA FLDALAVHRA GAGLAATAIA
     WGLWGEEAGI NAALDEVARN RFVRDGFRPV TTEEGLALLD AALASGRPAL AATPLAARTR
     SVRRAAAEKS TVDFATGLTA LEPAAREKVV LDLVRAEAAA VLGFPDTASV SADRPFQELG
     FDSLTAVDLR NRLGAATGVA LPATAVFDHP TPNALAAFVL DAAAPSGKSA VLTELDKLEA
     ALSGVGRDVR ERDGKEHAEV AARLRTMLVR WTETGDDEPD HEDAITSATT DEIFDFIDNQ
     LGRASS
//
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