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Database: UniProt
Entry: A0A2G0Q6K6_9GAMM
LinkDB: A0A2G0Q6K6_9GAMM
Original site: A0A2G0Q6K6_9GAMM 
ID   A0A2G0Q6K6_9GAMM        Unreviewed;      2065 AA.
AC   A0A2G0Q6K6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Polyketide synthase family protein {ECO:0000313|EMBL:PHM54836.1};
GN   ORFNames=Xhom_02793 {ECO:0000313|EMBL:PHM54836.1};
OS   Xenorhabdus hominickii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM54836.1, ECO:0000313|Proteomes:UP000225433};
RN   [1] {ECO:0000313|EMBL:PHM54836.1, ECO:0000313|Proteomes:UP000225433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM54836.1,
RC   ECO:0000313|Proteomes:UP000225433};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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:PHM54836.1}.
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DR   EMBL; NJAI01000004; PHM54836.1; -; Genomic_DNA.
DR   OrthoDB; 9757559at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000225433; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 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; IPR004432; Omega_3_polyunsat_FA_synth.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR02813; omega_3_PfaA; 1.
DR   PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR   PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 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; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 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; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          18..481
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          1233..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1019..1046
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2065 AA;  226658 MW;  056879519C6D8BB0 CRC64;
     MSESYLLHDG FLHDKKVRGD IAIVGMASHF PDAPNLYKFW ENIIEKKDSL IDITSKSEDE
     YWRKEDFYDP NPTVADKTYS HRAGFVPEID FDPVEFKIPP AIVDSISTVQ LFALYVAKQA
     MLDAGLIGQE NHKVNRDRIG VILGGAGNGN TSFSLASRQQ APYLRRIMMK AGLSEEVANE
     IIERTHGLYL EWNEDSFPGF LGNVACGRIA SHFDLGGTSY MVDAACASSF AAIKAAIGEL
     HSGSCDAVLT GGINLENSIF SFLCFSKTPA LSKSNLSRPF DQSADGMMLG DGVGMLVLKR
     LEDAELDGDK IYAVIKSLEA SSDGRAKSIF APRMEGQAKA LRRAYDAAGL MPSDIQLVEA
     HGTGTASGDD TELKSLHTVF GEYSTPPKSV AIGSIKSQIG HTRCAAGAAA MIKVALALHH
     KVLPPTINVD KPTHQLLAEN SPFYVNSEAR PWLRSFNGTP RRAALSAFGF GGTNFHAILE
     EYEKQTHGRY RLNESPWIML FKGADPAELL SQCEEALTCF SGHLPENAIR QHLEQQDIEN
     LKPQQARILF VAQSVEQAVE LLSIAIKQLR QNSASGWEHP RGIYYRPQGK ALEGKIVALF
     PGQGSQYVNM ARDIANDYPE MRQALETLDD VVISDLGHEL SPVIYPIPAF SDEEREAQQQ
     RLTDTANAQP ALGAISVGYF NILKGMGFTP DFVAGHSYGE VTALWAAGVL SDKDFYRVSL
     IRGRAAASAS ALRSTNTGGT NTDAGAMLAA SLAYEQRAEI LARYPDLVIA NDNSAQQVVF
     GGATSLINQL HDELKKHAVH CRILPVSAAF HTKFIQPAYP LYRECLADIN FQSPQCRLFS
     SATTEPYEHA SQAIRELLAE QLIKPVKFRQ TIEAIYQQGG RLFVEVGPKG VLGKLVADIL
     QHREHTVISV NPNDKGEERL QFARAQAQLL AEGIKLREIN QHVRPQPMTE DKSKRLTFKL
     TGGFFLSAKN QARRQHALRD DDRTTVEQFI AESVSASVPS APILQPRNTT ESKNEQAVES
     VVEKAVEEKE VEKEEVEKEV KTEIKTEAKN NQVASTQFIQ QNMLTIIQRR DNPMEQNNQL
     SENLDVNMVN VKTLNGLLQA QQVMSQLHQQ FQANQQEYIQ LLAMLLDKQY NLLESCKDHQ
     NLPTMLSSLS QSVQLLDKNL ELYHTNHERY FAVQQSLFQS GQIASVSSLT QSVVGYSATN
     VAPSAPMTVI EKVAPTVSVE PAPVSVSTVQ SPTIQSPTVA SPKVEPAKKP EKTETMMEIT
     PLRSTIPSMP KTEEILATPT MPSETVAAEP IKPAPVEAEV KVQAKVQTKV LDPEVEKQIK
     RFEQITEESI ISQLVAIVSE RTGYPEDMIT PEMDLEADLG IDSIKRLEIF GAMFDAFSAD
     AGIYHDSSKN KDLDTFDIDA LSNISKMAVF FKQMINETIE DLLNQGGDKT GSETLSSATE
     VVEERHSYED SKGHAADSGN SLGKLQTLGF FTTTVGSHGA DSVKKPLAEP QLSVSPAVQP
     ALNNQTVLNE QAVLNQAVLN EEASFADSPV SRFAVVKHSL PKPECLPGVF LSSKRWLVVD
     EGTNSADHLV AALRQQGQQV AVLTLGQNSI AMGDEAALSA TLTDIEQQQG TIEGVIYLQA
     PKLPVPEKSV NAVAEVFNER DYRSVETTFL LAKHLQGSLN HASPQVGYFI VVMRGDGELL
     TSGREYLPIV SAGVTGLTKS LNIEWGNVFC RTIDIDVRIK DNDVAQIVME ELQDHRTDLA
     EIGRSVNGER MTLALTEEKV LSASSVNQVN TSDVLVVTGG ARGITAQCVI ELAKQRQAAF
     ILLGRTDITV PLPEWAEGKT TLDERKMAAI AYLQAQGVQP TPVKINSMLD PLSHIAEINA
     TLQAIKQAGG RAIYLHCDIT NAEQVKMALS KAQQQLGQIT GLIHGAGNLA DKRIEKKTLA
     DLHSVFNAKV KGLENLCREL DCTSLRHIML FSSVAGFFGN AGQTDYSLAN EVLNKFVYLP
     FKGKNSQIVR SVNWGPWDGG MVSDVLKRAY EAQNMVIIPL EEGIQRFVRE FRDPRSCQIT
     LGGETYKAPK KTNISRNNNR YHSPS
//
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