ID A0A1A0TRR2_9MYCO Unreviewed; 1814 AA.
AC A0A1A0TRR2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OBB61521.1};
GN ORFNames=A5757_06745 {ECO:0000313|EMBL:OBB61521.1};
OS Mycobacterium sp. 852013-51886_SCH5428379.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834111 {ECO:0000313|EMBL:OBB61521.1, ECO:0000313|Proteomes:UP000091910};
RN [1] {ECO:0000313|Proteomes:UP000091910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852013-51886_SCH5428379 {ECO:0000313|Proteomes:UP000091910};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL Submitted (JUN-2016) 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:OBB61521.1}.
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DR EMBL; LZSU01000009; OBB61521.1; -; Genomic_DNA.
DR RefSeq; WP_066828357.1; NZ_LZSU01000009.1.
DR STRING; 1834111.A5757_06745; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000091910; 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; cd08955; KR_2_FAS_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 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; 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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
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:SF37; FATTY ACID SYNTHASE; 1.
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; 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; SM00822; PKS_KR; 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; 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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000091910};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1683..1757
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1814 AA; 194069 MW; F6FDF950D03F4ED4 CRC64;
MSTEPTTPAP LAIVGIGCRF PGGADSAERF WELLCSGTDA TRVVPETRWH GPRYHDPNPA
KIGKIVTDRG GFLSDIDQFD PQFFGISPRE AHSLDPQQRL LLQATWEALE DGGIPADGLA
GTDVGVFVGG FTLDYQLLQN QGRTSRYRFK SHSATGMMMT MLANRLSYAF DFRGPSMSVD
TACSSSLVAV HLAAQSIWSG ESVLALAGGV NIMVGPNTAI AESKSGFLSP EGRSKAFSDS
ADGYARGEGG AIVVIKPLEQ AVRDGDAIYA QILGTAVSQD GHTDGITVPR EDAQEAAIRS
ALRRAGVQPA DVAYVEAHGT GTPVGDPIEL RALGRALAAD RPASDPLLVG SVKTNIGHLE
AGAGVAGLIK AALVVDRGHI PANLHLDAPT RHVSLDELKI DIPGTGRPFP ARSRRIAGVN
SFGFGGTNAH VVLAEPPARE PIPAIDPSPA PVLLPISARS EEALLAVAGQ LAEHLDAHPD
VALDDLGYTL GRRRTHLNHR HTVVAETVAE ARERLHAVAD AGQLTTGRIA TTAPKLAFVC
TGMGPQWWRM CRGLLDVFPV FTDSIVRCDR ELSRYADWSL LEELRRDEDS SRMTETEIAQ
PANFAVQVAL AEQLAAFGVR PDAVIGHSAG EVAAHHLAGL LTFEQAVEVI YHRSRLQQRT
TGQGRMLAVG LDADTLMRTV DEKVLDEFGR RVSVAAINSP SAVTVAGDGD VLEDLARQLD
EAQIFNRHLA VQVPYHTHYM DQIRDELLQA FDGLSSKTAA VPLYSTVTGE RLDEYAAGAA
YWWQNTRATV LFEPAIRRML DDGYTHFVEI GPHPVLAASV FETAGQQRVS LTATQRRGHD
DARTLLDCVG ALHSHGHDID WEAVHSRPGR VLKLPSYPWQ TKRYWVETQE TTESLFYRPV
HPLLGQPVSG VHPTWEAEIS TLVNAFLADH RVQGSVVLPG SVYIEMAVAA AKATYGSHHS
VDNLVLHRAV LLDDTCDPIL RTTLNQDTGA LEFAAFTATA DGDLKWAITA TAELNTLPTA
PAGRGDHGTA EPVAEIDGGD FYARTEAIGF DYGDAFRSVR RVTAGEDWAI ADIAVPDGIT
AGLGDYCFHP ALIDGAFQTL FGAPFLGQKE SEDPYLPTRI RHCAVYGPAE ENMSVRVDVV
EATSEAVECD IIVSGAEGRT LAVFDGFVVQ SLSASSRMSA EHIDKGLYEI QWVPRIPDAP
EPVPATEADR SWLVLTDDHG VGAAVAGELT ARGQWVQTIG DAELVAAQLD SAGVAVGVVD
FRAVDQPEPE RGALAVLRLV KALIGRDGTT PRLHLVTANA QPAPGTSLSG VGQAAIWGLG
RVIGHQELGE YWGGLIDIDL ADGHAEIASH IVDQLLSDGA DDQLALRTGA AFVPRLRPCA
GLTKPFPTKL TPDATYVVTG GAGALGRVVA TYLAEKGARH ITLLGRSSIP PRSSWADLTE
GDPHFATVST IRAVERLGAH VATASVDITD ADQVAAWLRD HTRDGGRPVR GIIHAAGVVA
DQLLVNMDED DFVKVLRPKV TGTRILHEAF AGHDLEFFVM FGSAGSTIAA PGQGNYAAAN
AFLDAFAHHR QAQGLPALTI GWGPWSVGMV EELHLEKIYA HRGIELITPA VGGRILDRLV
NQRAANVVAI TADWGRARQA GLGGHLPAMF SDLQASGPTA AEDDSDASIL DVLAATPEAE
RRAVVADHVR RLVAAVFDTA VTDIEPDDML DDIGLDSMMA MDFRVRINTM FSIDLPVLEI
LRGVSVNSLA ERILTDLREV HADVPATDDA PDGQPVTDEG VDRLIEELSD DELRRLLAEL
EAQPAEPETG GATS
//
