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Database: UniProt
Entry: A0A132BVL7_9RHOB
LinkDB: A0A132BVL7_9RHOB
Original site: A0A132BVL7_9RHOB 
ID   A0A132BVL7_9RHOB        Unreviewed;      2153 AA.
AC   A0A132BVL7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Phthiocerol synthesis polyketide synthase type I PpsE {ECO:0000313|EMBL:KUP92421.1};
DE            EC=2.3.1.41 {ECO:0000313|EMBL:KUP92421.1};
GN   Name=ppsE {ECO:0000313|EMBL:KUP92421.1};
GN   ORFNames=TRIHO_27250 {ECO:0000313|EMBL:KUP92421.1};
OS   Tritonibacter horizontis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Tritonibacter.
OX   NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP92421.1, ECO:0000313|Proteomes:UP000068382};
RN   [1] {ECO:0000313|EMBL:KUP92421.1, ECO:0000313|Proteomes:UP000068382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O3.65 {ECO:0000313|EMBL:KUP92421.1,
RC   ECO:0000313|Proteomes:UP000068382};
RA   Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT   "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT   Tritonibacter horizontis.";
RL   Submitted (DEC-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:KUP92421.1}.
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DR   EMBL; LPUY01000075; KUP92421.1; -; Genomic_DNA.
DR   RefSeq; WP_068244647.1; NZ_LPUY01000075.1.
DR   PATRIC; fig|1768241.3.peg.2851; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000068382; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08953; KR_2_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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; IPR029058; AB_hydrolase.
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; IPR049490; C883_1060-like_KR_N.
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; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
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; PF21394; Beta-ketacyl_N; 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   Pfam; PF00975; Thioesterase; 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   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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   Acyltransferase {ECO:0000313|EMBL:KUP92421.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068382};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUP92421.1}.
FT   DOMAIN          14..442
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1773..1848
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2153 AA;  231644 MW;  C6D4C3E380B49AF5 CRC64;
     MGHSEQAFGT AIGPDDIAVV GMSVSLPGAA SVEAFWTNLR DGVESIEILD EDSLLQAGER
     PDVLRAPNYV AAAAPLQGFD MFDAEFFGFS PKEAAILDPQ HRKFLEVAWS AMEDAGHTPE
     SLKGQVGVYA GCGMGSYFYF NICSNPDLVD DVGMFLLRHT GNDKDFLTTR VSHVFDLKGP
     SVNVQTACST SLVAIHYAAE ALRKGDCDMA LAGGVTIELP QGRGYLFKEN EILSPYGHCH
     AFDHRAQGTV FGSGAGAVAL RRLSDAVADG DHIWAVIKGS AINNDGAAKA GYLAPSVDGQ
     SEAVRKALTA AKVHPESIDY VECHGTGTFI GDPIEVAALS EAYRERTDAT GYCRLGSVKT
     NIGHLDTAAG VAGFVKTALS LTHKTLPPSL GYEAPNPTID FDASPFRVND RLTPWVSHRG
     PRRAGVNALG VGGTNAHAIL EEAPVRAPSE ESDFPFQILC VSGQSKAALE ANTQNLVAYL
     RANPQVDLAD VAYTLKEGRR GFAKRRVVVA ETATEAADRL EAANPRAVFT HDRLGPAPEV
     VFMFPGGGAQ YAGMARDLYE TEPVFADWMD RGLDHLAQNL DFDLRAVWLP DPGSEASANA
     ALLTPSVQLP LIMIVEYALA QLWISWGIKP AALVGHSMGE NTAACLAGVL GFEDCIDLVH
     LRGQLFDTVD PGGMLSISLP LAEVEALIGM DLDIASVNAP ELTAVSGPNA ALDALAETLR
     ARDVEFQRIP IDIAAHSRML EPILTQYGDF LRKLDLKPAT LPVISNRTGQ LLSAEQATSA
     DYWVGQLRNT VRFADCIDTL SATPGRVYLE VGPGKALSAL AQMAPQVRAG QVLSSLRHPD
     QEVADDAYFF GVIGRLWACG VEADWPQIWG DSRRLRLPLP TYAFQRSRYF IEPGKAAATP
     EPDLPARHED LADWGYRPDW RPRLADCSAD LEAELRRTPL RWLIFEDSTG QAAACSARLA
     AAGHQVVRVR AGDTYAQLAP DLYQLAPEEG RFGYEALLAD LAEAALLPDR IGHFWLVTNA
     QEHRPGSSFF DRNVEMGLLS LTGLGQALAE ADLPQPVHIC VMTTGAAQVR DEALPTPEKA
     MISGPAGVLP REVAGVTVAI CDIELPEPPA GFAALLSRAP TTDISPRLLQ ELLAEPANST
     AAWRGSARFE LAYRATRLLA PERQDVPLQH GGHYLLTGGY GGIGLTVAEH LMRHYAARVT
     LVSREALPLQ ADWDSYLNRH SPQDRMARRI RAVQKLQSTG AGEVLTLRAD VCNLQDMRAA
     VDAAQAAFGP LTGVFHGAGH VADAPLLAKT ESQIAAVLAP KVSGLRVLDQ IFPDGALALM
     VLFSSTSTVT RPAGQVDYVA ANEYLNAWAK ARRGGQTRVI AIDWGIWAET GMAAEAMAAR
     QGRITLPDPS PCAAPLWHSR GFDTAGGAVF RSLFDARTDW LLNEHRTADG AALIPGTGYI
     ELIAEALHCQ GTSAPFEIRD LYFLQPFQVA DTAPRQAVLQ LAASDPGYRA RLHAGTPEGY
     VTTAEAQVAP LAPAPAIGVV SLDQIRDRCK KRSAAPEGGR LRSPQEANLR FGPRWHVLQE
     TALGDGEGLA HLRLPDLAQK DATLLHPGLM DLATGWAISL APDYAPETLW VPVSYGAIRV
     FSALPHEIYS HVRLVAEDEA PGTALFDITL TDPTGQVLVE ITHFRMQALT GGFGLQPART
     SVSAIALGLE AETEIQPLSP DERRLVANLE NGIRTADAGN ALERALAQED PQIIVSSLDL
     PDLIRQAQSS GQIPPSSTSQ SFERPDLDTD YVAPRTALEE TLAGYFGALL GLSQIGVEDS
     FFDLGGHSLI AVRLFAQIKR ELGLDWPMSV LFEAPSVASL AARIEAESDQ PGRGNNGVAS
     EEPAGDAPVF KHLVRLHPGK VPDARPMFIV AGMFGNVLNL RHLAQILGED RPVYGLQARG
     LVGADAPHDR IPDAARDYIA EMRHIQPDGP FLVGGFSGGG ITAWDIAQQL RASGDAVDAL
     VLLDTPLPVR PSLTAPDKML IKLAELRDKG AGFVAEWARN RVAWEIHKRQ APPTDQNTGT
     GFNNRKIEQA FRTAIATYAP QVWDGPVTLY RPALDRQWKV TGGRWVSTER EYVYPDNDWT
     RFAPNLKVVE VPGDHDGMVL DPNVSVLGKA IRALLAQTAR GSQTAPDRAR AAE
//
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