ID I0UWV2_9PSEU Unreviewed; 1905 AA.
AC I0UWV2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Polyketide synthase family protein {ECO:0000313|EMBL:EID52355.1};
GN ORFNames=SacxiDRAFT_0070 {ECO:0000313|EMBL:EID52355.1};
OS Saccharomonospora xinjiangensis XJ-54.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882086 {ECO:0000313|EMBL:EID52355.1, ECO:0000313|Proteomes:UP000004691};
RN [1] {ECO:0000313|EMBL:EID52355.1, ECO:0000313|Proteomes:UP000004691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XJ-54 {ECO:0000313|EMBL:EID52355.1,
RC ECO:0000313|Proteomes:UP000004691};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "Improved High-Quality Draft sequence of Saccharomonospora xinjiangensis
RT XJ-54.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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DR EMBL; JH636049; EID52355.1; -; Genomic_DNA.
DR STRING; 882086.SacxiDRAFT_0070; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_5_11; -.
DR Proteomes; UP000004691; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 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; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF08659; KR; 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; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1750..1825
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 68..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1905 AA; 197911 MW; 0BC115E9800BC096 CRC64;
MVMAMWHGVL PRTLHVGEPT SQVDWSSGAV ELLTESRPWP EVDRPRRAAV SSFGISGTNA
HVILEQPPAH DSTHDSTHES DAEQPTHGAT EAPSSTPPWV ISGGSAQALR AQAARLLERL
AADSEWSPVQ VAVALTRSRA RLDHRAVVLG SDRAELLAGL TAVADDRDAP GVVRGTARQT
GRVAMVFTGQ GSQHAGMGRE LYEHYPLFAA AFDEVCAELD PLLGFSLREA VFATEPAQPP
GARTIDDTGL AQPALFAVEV ALVRLLESFG ITPAVVAGHS LGELTAAYVA GLWSLPQACR
VVAARARLMQ QLPEGGAMAS VAATADEVRI GLLELDATPD DHGRDIETAL VARVGVAAAN
GPSSTVISGE ADAVERVLRW WQDRGRRVRR LPVSHAFHSP LTDPMLDDYR LALADVEFGA
AALPVVSTVT GTLLSRSDAA DPDYWVRQVR EPVRYVNAVH TLAELGVTTV LEIGPGSVLT
ALTRDTLDHM DPTGSAAASP VCLSLLRSDR GERAALLTGI AASLAHGVPV DLSPLLPAGA
APADLPTYAF QRERYWLDVS RMPTDAAGLG LVSSGHPVLG ARVDLPDSGA VVFTGRLSTA
ALPWTADHQV GPAAVFPGTG LVDLVLAAAV DLRSPMVDEL TLHSPVVVPA EGGLAVRVRL
DRLDDHQPDQ SADGAATPIG ERARDSERVV TVYTRPEGDP TAEWTSHATG RLVEAEPASA
PVGETGRESW PPPEAVPVST DGLYAAFEAA GLVYGPVFQG LRAAWVAADT VFAEVELPEP
AWREAPAYGV HPALFDAALH ALGLTDAVGV LPSGDAGEAK GVRLPFSWAG VRIHAAGATR
LRVTLRTVED GDVEVRAVDA DGAPVVTVDR LTLRRAVTGG RPATSAFDIH DALFDLDWVP
TSPADPPADA GWWALLGSID EGLTGGLVAA GVSVSSVADL ADVSARVTTG EAAPSVLVVP
GGALARTGAA PEMIDDVRHA VERMLDVLRT WSAEEHLASS HLLVVTRGAV ATGETDGVPD
LAGAAVWGLL RTAQTENPGR ITLLDLDPAS SDPDAVGALA ACLSGVPRLA GGADVQYALR
GGRVLTPRMA PLRVLQPGQD GRTDQGEQVA AADVTGPGGL VADDRPASDD VIVTGGRWRV
GVATPGSVAG VGPLPSAGSP TGDAALAPGE VRIAVAAAGL NFRDAMAALG MYPGVVEIGG
EGAGTVVEIG ADVTDVALGD QVMGVLPGAF AASVAVDRRM VTPLPAGWTA VEGAAVPSVF
LTALYGLAGL AELSAGQSVL IHAAAGGVGA AAVQVARSKG ATVFATASPG KHQVLRDWGI
PDERISSSRD LDFESSVLAA TGGRGVDVVL NALAGPFVDA SLRVTAPGGV FLEMGKTDLR
DPAAIAEEYP DITYRPFDVS ALHPDVVAAL LTELRELFDR QVLMPPPITE YPLRHLRPAL
RALAGAELIG KAVLRIPRPV PPNRTVLITG GTDGLGRIVA RHLVTRHGVA SLALLSRRGG
DTPGVADLVA DLQAAGARVT VHAGDVADPK AVAEVIDAIP PEFPLAGVVH AAGVLADGIV
SSIDAERAAR VLAPKVAGAW NLHRATEGLD LSLFLTFSSV AGVWGAAGQG AYAAGNAFLD
ALIARRRALG LAGTSLAWGP WTAETGMTAG LAATDQHRLH RWGLRPLAPH DALELLDTAF
TTRPVLAVAA AVDLAALGRR AAEEVPAVLR GLVRGPGPFA TPRSTRPAET GSPSRWMAEI
AALPRSERHH RVTTLVREAV AAVLGHARAD RVGQTQSFGD LGFDSLTAVE LRNRLRAATG
VTLSATAVFD HPNPAELADR VLRGLALPED DPTRDVLRGI DDLEAGLALL TPDDDHAQIT
ARLQNILWRL ADAGSAAEPS SPERLTEASP DELFDFIDRE FGELT
//
