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
//