ID A0A1V2TA81_9NOCA Unreviewed; 1408 AA.
AC A0A1V2TA81;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:ONM46409.1};
GN ORFNames=B0T46_23185 {ECO:0000313|EMBL:ONM46409.1};
OS Nocardia donostiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM46409.1, ECO:0000313|Proteomes:UP000188836};
RN [1] {ECO:0000313|EMBL:ONM46409.1, ECO:0000313|Proteomes:UP000188836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1655 {ECO:0000313|EMBL:ONM46409.1,
RC ECO:0000313|Proteomes:UP000188836};
RX PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA Potter G., Perez-Trallero E.;
RT "Nocardia donostiensis sp. nov., isolated from human respiratory
RT specimens.";
RL Antonie Van Leeuwenhoek 109:653-660(2016).
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:ONM46409.1}.
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DR EMBL; MUMY01000025; ONM46409.1; -; Genomic_DNA.
DR RefSeq; WP_077120945.1; NZ_MUMY01000025.1.
DR STRING; 1538463.B0T36_05935; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000188836; 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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd06454; KBL_like; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major 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; IPR004839; Aminotransferase_I/II.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; PF00155; Aminotran_1_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 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; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
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 Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000188836};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..422
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 914..993
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1408 AA; 150286 MW; 8F30D0FEFF37CD74 CRC64;
MTDIAIVGLD CRFPQAPDPA ALWQLLIDGR DAITEVPASR WNADDFHDPA GAPGTINTRS
GGFIDDADAF DHQFFGIPPR EAEAMDPQQR LLLQAAWRAF EDATLDPRTQ AGSRTGVYIG
VMANEWANLQ MRDYHDYTAI TPQHGSGNGY FMTANRLSYQ LDLKGPSVAV DTACSSSLVA
IHLACAALAN GECDQAVAGG VNLVLTPAVG VFYTQAGLSA PDARCKPFSG DADGIVRSEG
VAVLVLQRLA DAQAAGLPIY AVITGSAVNS DGRSNGITAP NRWAQQQVIG EACQRAGITP
TDIDFLEAHG TGTVLGDMIE VKALGALHST NRARPCGIGS LKGNLGHTEG AAGIAGLIKV
ALSLHHNTVP PTRCADQENP KLRMQQHGLR LLAEQMPLTS PAYGGVSSFG VGGTNAHIVL
ESAPTTEAPG TPGGGVLTLS STSEDGLRRN ARRLAAALDS APRNHFAQLC WTSNHVTSSG
RHRLAIAATD RDDAIAQLHD NPATGTAGPV DLGWMFTGQG TQYTGMATAL HRTNATFRGA
LARVDHTMTA HLGRSVRNLL LDNNTDIDRT ELTQPAIFAM QYALAETLTA TGIQPAWLIG
HSIGEFAAAT VAGVFDLDDA CRLVTARGRL MQRLPDGGTM LAVRATPAAV ADLLAHEPAV
ALAAINGPRD LVLSGDGTAI TRIRAVLTDR AVSTRTLTVS HAFHSPLMEP ILGEFEAVAR
NCTYRPPQLP VYSTVHGRLL DTHETMDAAY WTEHIRATVR FGDAITAALT TEPSHIIEIG
PRRVLATLLG RIRPDMQARC LTPSPGPAAT GHELTETLAA LYRDGFNPDW DQLYEPTQHV
RRRLPVYEFS TEHRFWIEPD TLIAPTTPAP QPEETAMDQM IALFREQNAV LARLLGTPTG
EVTAPQPDTT QATTDQNTVA AVVRAELARV SGFPAERIRD NHTLTDGLGF DSLMLTDLSG
GLVRKLPGLT IDPSTFTATT TLGDITTYVT NQVTEPPAAP EPPTITPEYQ ISDFAEVKAI
ADRISGAESL GLTNPYFLVN DGITADTSLI DGKPVINFSS FNYLGLSGHP AVTAAVQDAV
ARYGSSCSAS RILSGEKPVH RELETELATL LGTEDAIALV GGHSTNVTVI GHIVGPQDLV
IHDSLAHDSI VQGCTLSGAT RRPFPHNDHA ALDRLLTDIR HRYRRVLILI EGIYSQDGDI
PDLPAIIAVK KKHKALLMID EAHSIGVLGA HGGGIGEHFD IDRNDVELWS GTTSKALAGC
GGYVAGSAEL IRFLKYTTPG FVFSVGMTPM NAAASAAAIR QLRTDHEPLD RMHRNARLFL
RLAREAGINT GDSNDTPIVP CIVGDSRTAL KLSHALLNRG INANPILYPA VPENLARLRF
FITACHTENQ IRDTIKILAE ELALLTGP
//