ID A0A370BDS5_9ACTN Unreviewed; 1582 AA.
AC A0A370BDS5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=SDR family NAD(P)-dependent oxidoreductase {ECO:0000313|EMBL:RDG39791.1};
GN ORFNames=DVH02_01765 {ECO:0000313|EMBL:RDG39791.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG39791.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG39791.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG39791.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:RDG39791.1}.
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DR EMBL; QQNA01000009; RDG39791.1; -; Genomic_DNA.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000253741; 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; 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 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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR015083; Polyketide_synth_docking.
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; PF00550; PP-binding; 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; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 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 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:UP000253741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1430..1505
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 459..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1582 AA; 165531 MW; C41F44B1C9337E14 CRC64;
MAGGAMATSS EAVVEALRAS LKENERLRNA ARAAVEPVAI VAMSCRYPAG ANSPERLWDL
VVDGGDAVSG FPGDRGWDLT SLFAADPEQR GTSYTREGGF LYDAAEFDAG FFGISPREAL
AMDPQQRLLL ETSWEAVERA GIDPLSLRGS RTGVFAGVMY HDYGARPGLP TEEVEGYLGT
GSAGSVASGR IAYTLGLEGP AVTVDTACSS SLVALHLAVQ ALRRGECSLA LAGGVTVMST
PSTFVEFSRQ RGLAPDGRCK SFADSADGAG WSEGAGVLLL ERLSDARRGG RRILAVVRGS
AVNQDGASSG LTAPNGPAQQ RVIRQALDDA ALSATDIDVI EGHGTGTPLG DPMEAQAILA
AFEGERERPL WLGSVKSNIG HTQAASGVAG VIKMVMALRH GVLPGTLHVD KPSTQVDWSA
GTVELLTGTR RWPDPGRPRR AGVSSFGISG TNSHVVLEEA PADDRERPAP APGGPLPWLV
SGRSGAALRE QAERLLRYLE GEPGPRLTDV AFSLATTRSA FEHRAVVVAG DRAELARGLR
RLAAGELPAE GARGEVREGA LAFLFTGQGA QRVGMGRELY ERYPVFAGAF DDACAALDRH
LDRPLRDVVF GAAGTDGLLD GTAMTQPALF AVEVALHRLV ESWGVRPDFV SGHSVGELTA
AHVAGVLSLA DAAVLVAARG RLMRALPEGG AMTAVQATEE EVAPLLAERA GRAGLAAVNG
PSAVVVAGDE DAVGEVASYF SERGRNTKRL RVSHAFHSHR MDPMVAEFAE VVRGVSLNAP
RIAVVSALTG AVVTPEELCE PEYWARHARD TVRFLDAVRT LEAEGVTAFL ELGPDAVLAA
MGQECVLGDD AVFAAASHRD RPERTALLAA LGGLHVRGTE VDWAGVLDGG DGRWVPLPTY
AFQRERFWLA AEDGAERSLA RVDEHRYRVD WAALPDPGAA PLSGRWLVVS AAGAEGPAAE
TAAACRRAGA AEVVRLTVDT GTGTDRALLG RRLREALGEG PPVGAVVSVL ASDERPLPDG
PALSGGLAMT VVLGQALGDA GVDAPLWCLT QQAVAVGPEP VRNPAQAAVW GLGRVAALEW
PRRWGGLVDL PGEVDETALS RLVSIFANPN GESQLALRAS GVHGCRLVRS PLAQAPVRRA
WQPTGTALVT GGTGALGAHV ARWLAGQGVP HLVLLSRRGR DAPGVAALEA ELTGMGSEVT
VAACDLTDRE DLRRVVDALP EERPVTTVVH AAGANHGEKP LARCDLTEIA EVMSGKLEGA
RNLDAVFDGS APGRSPDAFV LFSSGAGVWG STGQAAYAAA NAFLDALASA RRAGGQAATS
VAWGAWGGGG MAGAEGAGES LRERGVPLMA PETALAGLRA TLDRDETTSA FAAVDWSRFA
PVYSMSRSRA LLDDLPDARR ALRVESGSGP ERAGSLREEL TRLTADEQER LLLDLVLAQA
ADALGHRTRD AVRATSAFKD LGFDSMASLT LRNRLNEATG LALPTTVVYD HATPVALARQ
LRAEVLPQGG SGAVFAEVDR LETAVEAMGP GDEARGRVVA RLRTLLWKWD QPDPTAGEPD
DALTSATDDE IFRIVNKELG IS
//
