ID A0A0M2JZM8_9MYCO Unreviewed; 1477 AA.
AC A0A0M2JZM8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KKF02084.1};
GN ORFNames=WN67_10145 {ECO:0000313|EMBL:KKF02084.1};
OS Mycolicibacterium obuense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF02084.1, ECO:0000313|Proteomes:UP000034150};
RN [1] {ECO:0000313|EMBL:KKF02084.1, ECO:0000313|Proteomes:UP000034150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|EMBL:KKF02084.1,
RC ECO:0000313|Proteomes:UP000034150};
RA Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium obuense UC1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKF02084.1}.
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DR EMBL; LAUZ02000038; KKF02084.1; -; Genomic_DNA.
DR RefSeq; WP_046362901.1; NZ_LAUZ02000038.1.
DR STRING; 1807.MOBUDSM44075_03682; -.
DR PATRIC; fig|1807.13.peg.3379; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000034150; 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 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; 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; PF00668; Condensation; 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; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..445
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 927..1001
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1477 AA; 157173 MW; 44C896103029E1A7 CRC64;
MTSSTGEQEI PDNAIAVIGM AGKFPGADSV SAFWRNLRAG VESIVDLSES ELLANGVTER
ALANRGYVRR AGLMPGIEEF DADFFGFTPY AARMLDPQHR LFLQAVFHAL EDAGYDPHGL
ESTVGVFGTS SSSGYLLHNL MSNFDPMMVI GQGASFEMVN LSLQNDKDHL ATRVAHQFDF
RGPALSVATA CSSSLVAVHL ACQSILNGEC DIALAGGSSL RIPHHVGYWY EQGAMVSPTG
QCRPFDVRSD GTIFASGVGV LALKALPDAI DDGDRIHAVI RGSALNNDGA TKMTYAAPNA
LGQAEVIAEA HAIAGVDASS ITYVETHGTG TPLGDPIEVE GLRQAFELAE ETRSAPCYLG
SVKSNIGHLE TAAGIAGLIK AILCLEHKAI PATLHYTSPN PELHIDRGPF RIRNADGPWE
SDGIRRAGVS SFGVGGTNAH IVLEEAPLRP APTPSAKPQV LVLSARTQEA LAQSRAALAT
ELADSDDVSL PDAAYTLTRR RKDPFRLAAV VHDQANAATV LSATETDNVF EGQGVTDAEE
SGDRVAFLFP GQGAQHIGMA RGLYDTEPVF ARHFDECVAG FNGLMGYDLR AEIFDGVGRN
LEHTDRAQPA LFTVEYALAK LLQSYGVEPA IMAGHSIGEY AAATIAGVFD LDTAIKVVAK
RAQLMHAAPR GVMVAVPLSP QAVAEYLTGD VDVATINDPG SCVVAGSDEA IRTFQAALAE
KGVAARRVRT SHAFHSRLMD PVVAEFSSFL SGVTLNEPRI PLLSNITGTT MSTAEATNPN
TWARQIRATV RFADELDLLL SAPDRVLVEV GPGGTLTSSA GRHPRWSERH RAVRMMRHQA
QNRSDGDTFL LGLGQLWAAG VDVDWTPAWT PGSNDDAEPQ LVTLPGYPFA KQRHWVEHNA
NAAWLNGSPN GVALDGAAPA AAPAAAGGAS SVETVLAQVW AQCLGLPDID RNANFFEIGG
DSLIAISVAM TAGHRGLDLT PQDLYENQTV SSLAKVLSAR YAEGGLARQS LDDVVTPPVP
PNVAYFLEHG LRDVGRWRTP VVLGLRADIG EDDVRAVLTA VSAAHDALRV HLVERSGTWE
QHIAEPGEFT ELIVRALPDG VAAGSPQERE AVHAALDEQV REHQLLTAPL TATFLRGAHG
SRSHLALTLH GVASGPGDDG TSRDVLLTDL VTAFSQRMAG EEITLAPVPT SWREWSQRCA
GLATHPAVLD SRDYWLQVAR AATVTVAGPE PSERPGADDL VRLSSALSPA ETGEIDDTRR
RLRLPVEEIL LAALGRTVAA TVGDGTVAVD LGGRGRSVLK PDVDLQRTVG WFSTLHPVAL
PAAQQTSAPA LLDDVRETLK AVPHYGIGYG LLRYLYAPTA RALADTRSAD ILFTHVGTIP
DVPAEQPDDA AVRFDADTAL PIRDALPGLG HALELRVYRS AGVLYLDWWY DSRRLGPTDV
ESFARQYSTA LLAITREAQA AEDADAAGDE LALVDLS
//
