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
//