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Database: UniProt
Entry: A0A0N1G4G9_9ACTN
LinkDB: A0A0N1G4G9_9ACTN
Original site: A0A0N1G4G9_9ACTN 
ID   A0A0N1G4G9_9ACTN        Unreviewed;      1573 AA.
AC   A0A0N1G4G9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   23-MAY-2018, entry version 15.
DE   SubName: Full=6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:KPI10575.1};
DE            EC=2.3.1.94 {ECO:0000313|EMBL:KPI10575.1};
GN   ORFNames=OK074_3106 {ECO:0000313|EMBL:KPI10575.1};
OS   Actinobacteria bacterium OK074.
OC   Bacteria; Actinobacteria.
OX   NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI10575.1, ECO:0000313|Proteomes:UP000037991};
RN   [1] {ECO:0000313|EMBL:KPI10575.1, ECO:0000313|Proteomes:UP000037991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK074 {ECO:0000313|EMBL:KPI10575.1,
RC   ECO:0000313|Proteomes:UP000037991};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074
RT   OV450 and OV320.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPI10575.1}.
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DR   EMBL; LJCV01000220; KPI10575.1; -; Genomic_DNA.
DR   RefSeq; WP_054216489.1; NZ_LJCV01000220.1.
DR   EnsemblBacteria; KPI10575; KPI10575; OK074_3106.
DR   PATRIC; fig|1592327.3.peg.5042; -.
DR   Proteomes; UP000037991; Unassembled WGS sequence.
DR   GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.40.366.10; -; 2.
DR   Gene3D; 3.40.47.10; -; 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; IPR032821; KAsynt_C_assoc.
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; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; IPR016039; Thiolase-like.
DR   Pfam; PF00698; Acyl_transf_1; 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; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF51735; SSF51735; 2.
DR   SUPFAM; SSF52151; SSF52151; 2.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:KPI10575.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037991};
KW   Phosphopantetheine {ECO:0000256|PROSITE-ProRule:PRU00258};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW   Transferase {ECO:0000313|EMBL:KPI10575.1}.
FT   DOMAIN     1445   1520       Carrier. {ECO:0000259|PROSITE:PS50075}.
FT   MOD_RES    1480   1480       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   1573 AA;  167827 MW;  51D185969FF2D3C1 CRC64;
     MTDRPYDDSA LQGRIAVVGL DCRLPGARNP AEFWHNLLAG TDSISDVAEE QLEAAGVPAR
     QRADARYVRR AAVVEDTDLF DASFFYLSAR EAERMDPQLR LFLQSSWTAL EHSGHDSEQY
     AGRIGVFAGS LSSTYLLDNV LTGERGFKGS VRAMRQDLAT MMGNDPNYLA TRASYHLNLT
     GPSISVQTAC STSLVAVHTA AQSLLSHECD VALAGGVALR FPQEAGYLHE TDGIASATGT
     VRPFDAGADG TLFGNGVGVV VLKRLEDALA ENDTVWAVLC GSAVGNDGAD RAGYTAPGVS
     GQAAVLAEAL AVADVAPESV TYLETHGTGT LMGDPIEFAA LAQSYQVDGA PPLRLGSVKA
     NVGHLSAAAG VTGLIKCVLM LHHRTLVPTP HFTEWNPECE VEGTRFRMGT AVEPWETAGG
     PLRCAVTSTG MGGTTAHTVL EEAPAHRAGD RAGAAGGGLV VLPVSAKSPA ALETARTALA
     DHLETTAPEG ADPGLADAAY TLATGRRTFN YRAVVTAPDR ATAVQALRTG DPRFVHQDSG
     QPADRPVVLL FPGQGAQYPG MGQGWYEQLP VFRAVLDECA QLLLPRLGFD LRDALYPELR
     GYEGERHDLN RTRLTQPALF AVEYALARQW TTWGIRPAAL IGHSIGEYVA ATLAGVFSLP
     DALHVVAERG RLVDELPGGV MASVMLSPAE LEGYLDDDVA LAAVNEPAVC TVAGTREAVG
     RLTARLTADG VAHRKVVTSH AFHSPMMEPA VEQLTEVLRQ IELRRPHIPF LSNRTGTWIL
     DDEATDPAYW GGHLRATVRF ADDLATVLAE DRTVFVEVGP GQTLATFTRR HPDRETGVPV
     LTSAARGRAA TDVTAVHAAL GRLWAAGLTV DWAGYHGGQD RGRVPLPTYP FEGVRYWVEP
     GAAEVSGTRG GTAAPVGKLP VDEWLSAPVW RQAVGALDAP VEPLGEPVLL FADADGVAAR
     LTEHAFAGEV FTVAAGDAYA RDGDTWTVRP DSEEDHGRLV ADLLAEDRLP ARVVHAWAAG
     QLPAERGIER FEQAQRTGLY SLIALVKALS AQGVTRPLQL DVVSAGAYAV SPAEPEPASE
     LVTLGVAARV VGQEHGNIGS RHFDLPAPVD ERSLRTLAAE LTGFRRPEVA VTLRGATRWT
     ADMAPVRADW TATAQSRLRE RGVYLITGGL GEIGSTIARW LHGECGARLA LLTRDALPPR
     EGWDDWLGGH DADDETALRI VRLRALEAAG AEPFLVNADV ADEAGLRAAV ERVEAHFGAL
     DGVVHAAGLP SEQWDRAITA ASVEQCQWHF VPKAHGQIVL EKVLADHPVD FCLLLSSLAG
     VLGGLRLLGY GAANHFMDAA AERANRGLDR TVWISAAWDV WQHHQDEKRA LSAIGRSMDD
     KAIQPDEGLE VIRRLLTLRD ISHVAVSTWD IGHRLDQWVR DDRVARPSAG VAAEPDDAAA
     GLSSDGDRDL TEQVTRMVRH SLGTEDITPD GDIFEFGGDS LLIVKLLSDV REQFSVEVPL
     ADVLGEPTSR ALAALVQERL DDRRDSGPSA PGDDEVDELA AELAALGADE IERLLAEAEA
     GPDAARTAGE QEH
//
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