ID A0A068QX34_9GAMM Unreviewed; 1670 AA.
AC A0A068QX34;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative polyketide synthase type I {ECO:0000313|EMBL:CDG18410.1};
GN ORFNames=XDD1_2711 {ECO:0000313|EMBL:CDG18410.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG18410.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG18410.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FO704550; CDG18410.1; -; Genomic_DNA.
DR RefSeq; WP_045971622.1; NZ_VNHN01000012.1.
DR STRING; 351671.XDD1_2711; -.
DR KEGG; xdo:XDD1_2711; -.
DR HOGENOM; CLU_000022_16_14_6; -.
DR OrthoDB; 6437095at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000032721; Chromosome.
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; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
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 PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..436
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1118..1193
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1670 AA; 183830 MW; F9E91F67C73F6BBD CRC64;
MSAEIREDLD IAVVGLAGRF PGAENGTEFW RNLLMGVDGI SRFTEEELLQ AGHDIKKIGH
KDFVPVNGVL EGANYFDAAF FGYSQAEAAL LDPQTRLMMQ CVWHALENAG IDPAKRGRNI
GLFLGARSTI PWTMQAMLSE QVENVGGFLA SQLANKDAMS TLISWKLGLE GPSFTLQTAC
STSLVSVHQA VQSLLSGECD FAVAGGVSLL LPQQNGHTYQ EGMLFSKDGK TRAFDAEATG
SVFGSGLGAV VLRRVGEAIA DNDPIWAILK GSAINNDGTR KVGYTAPSVK GQADVIRTAL
QMAEVDAADV DFIECHGTAT SLGDSIEFMA LREIFNQSRS FGVNQCALGS VKTNIGHLDS
AAGIAGFIKM VMAIRYGVIP PTLHFQSPNP QLGLEQSPFY INTCAEPWPA KSGKLRIGAV
SSFGIGGTNA HIVLQQSIFA SAISRPERGG NGDKTYYFPF SAKNKASLAL QLESVSHWLV
QQSYLDLHAL SHTLSQRHCF SCRIMFIADA KFVLMQQIKT YLELEEEDDE LALIPQFLAK
GAVPADERTE ILAAIRGWIS GQTQEPAKWL FPPFDGQPLI DVPGYAFIRE DHGAGHITDK
RWAQISAVIA ATDGNNLSRN SAGLLLPFWK PHRLPKVPLP EKTAEKTSHS LLLIDQLLLD
RALASQARAW VDSSQIETVK LNILCPKQVR NALVGLSPGL HKNRALVLSL AFPADGFSFA
PDSLQTLSEL GKVLAESDFS AFNSVHIYLI ASAVIGDGND SAESVLTEAA LKALALVLPQ
EIPGIDCAFL SLQEPNADAL TRLLQTPLHG PLKLNSEGLF VEDFRCPDAE ENEVVDESDF
MGKTYVITGA GGRMAKAMAK VIAQRFQGRL ALISRQSADS AAMQRLLLEL KEDGAGAVEI
FPYALEREEA ALALFESIRH RLGDIHTVIH AAGVTEGDSF SPLVTLNAEH YRAQLQPKAQ
VAAVLANVFE SIPVEYCFMT SSMSVFFGGI AHAPYATANL FLDGWGQRQN RQPQNPRWIV
VNWETVHFDE QSRPTEILTW GSNEVAFSAA EFPALFERSL REYDRENQKI FSAGQFMDRL
YAWGGRRIAN GNGNSKRQVT NSIKLKPRPE TLPSVYQSPV NETQKEIAAI WSQILGIDGI
GIDDKFMALG GDSLKTIVMA EKVYKKLGKR IAIQDFFAQP TIREIERQFL HEQEYSPSML
PAIDLYDPIV ASADQDLLYI HQITFANGSY NMPMAFRCPR SVSATSIARA IEQVADRHPV
LKCLFERQGA DLMMLPQRDV TVGMLISEAG DKPEENLARL QQFANMPFDL HTELPIRAMM
LTGSEGLPFH QVLIVVHHIV CDAVSLGILA DDFQRLLQEL PLPVPEYSFA AYRRDRQASE
SKDKVRKEKA YWLANLLPLP APLSLPVAEG YDWHTDTEKA RGITLESDLS PQTSIEIRRL
CDELGLPPFV FFLGAFGVLI AKITRADAFL LGVPVTGRMQ PEELALVGYL VNMLALKMEP
ETDLPVADYL LQLHAQWAES IPYQTYPMSA LLDDLSAERQ LQNRQGKHPL FDVVFGYLPV
SLSGADENND INGESGFSRL ELTLEAVKFD LAMDVSETRD AFNCTIQLRQ PMFSETIGKA
ILDYFFVLID EIIANPEEEI QELLKNLNHG HTPELFAQAN DQDIESEFNF
//