ID L0DLZ0_SINAD Unreviewed; 2432 AA.
AC L0DLZ0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Polyketide synthase family protein {ECO:0000313|EMBL:AGA29701.1};
GN OrderedLocusNames=Sinac_5564 {ECO:0000313|EMBL:AGA29701.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA29701.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA29701.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003364; AGA29701.1; -; Genomic_DNA.
DR STRING; 886293.Sinac_5564; -.
DR KEGG; saci:Sinac_5564; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG2070; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_30_1_0; -.
DR Proteomes; UP000010798; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
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; 3.20.20.70; Aldolase class I; 2.
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; 2.
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; IPR013785; Aldolase_TIM.
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; IPR004136; NMO.
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; 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; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF03060; NMO; 2.
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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 654..1105
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1753..1837
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1586..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1843..1871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2432 AA; 256355 MW; AB4245FA1830A973 CRC64;
MGILDRGFDF RAEVDLEVLH RTSKFLKGQT FGLRLSACAL DEAVVASFPS NLGMVAVVEA
GGEDWSRLRA ILSGSDRVAV AEVTSRESCR AAAEAGFEAL IVAGNEAGGR VAEESSFILL
QAALGINNAP PVWVRGGIGL RSASACVAAG AAGVVLDGAV LLAKESPLQA SLRRRIERWD
GSETILVGRE VGDLLRIQAE PGSPALARLK QAATEGRLAW ESALRREVGW SEGQVRPVGQ
DAALAGGLAR THVTVGGIVQ AVERAIDLGL RDARSARPLD EDSPLARSHR TRYPIVQGPM
TRVSDLAAFA EAVAEGGALP FLALALMRGP EIGRLLTETA ARLNGSAWGV GILGFVPPDL
RLEQIEEVRR ARPSFALIAG GRPDQAQELE REGIATYLHA PSPGLLRQYW NDGARRFVLE
GRECGGHVGP RSSLLLWEQA VEVVHEMLEK GGTPDEVHLL FAGGIHDARS ASAVAALSGP
LARRGVRVGV LIGTAYLFTA EAVATGAIVA KFQDEAVRCT ETVLLETGPG HEVRVSPTPY
VEAFELERKR LLAAGRSNEE LRTALEGMNA GRLRIAAKGI ERNNGAGSPL VGVAAESQTT
RGLYMLGQAA TLRQGVSTIA ALHQDISAGG MGRIDRLADA LAASEPLASS KAEPCDIAIV
GMSAIVPGAG DVRTFWENTL HGIDAITEVP ADRWDWRLYY DADPKAPDKI TSKWGGFVPE
IAFDPLRYGM PPTSLPSIEP LHLLTLEAVR AAIDDAGYRD RPFPREKTAV VLGAGGGAAQ
LAMGYAFRSY LPMLDTLAPG AGREALEQCE GVLPEWTEDS FPGILLNVAA GRVANRFDLG
GANYTVDAAC GSSLAAASVA VRELESGAAD VVILGGADTV QNPFTYLAFS KTHAFSPRGR
CRPFDASADG IVISEAVAVV VLKRLADAER DGDRIYSVIK GLGASSDGRA KGLTAPRPEG
QIRALRRAYA KAGIDPATVG YVEAHGTGTA AGDLAEVNAL NDVFIESGAP EGRCALGSVK
SLIGHTKCAA GLVGLINASL ALHHRVLPPT IGVVNPSAQA SRPQSPFHIS TKTRPWIHTD
EERPRRAGVS AFGFGGTNFH AVLEAYEGAP AAASAPLRDW PAELFVWRAA DRTLLLADLE
RLSLALEQGA KPALRDLAHT LLNSLGATGL SLAIVASTLD EVRAKVDQAR ATIAQGVAEF
HDPRGIAFAE AASDSLNRVA FLFPGQGAQR VDMLGELAVL FPEVRSGFES FDNVLREQGK
PLVSPVVFPP PAFQAEERDR QKKALAETEV AQPALGGASL GLLWLLESLH VAPDMVAGHS
YGELVALHAA GVYSLEALVR LSEARGRFIK AAAGDQPGMM AALAASPDQV ETLLQGLEGV
SAVNWNGPRQ TVVSGRSDAV AAALGRARQS GLRGQELAVS CAFHSPIVAG ACRPLAELAN
SLAPQSPQCP VFSNVTGTRH TDDPTAIAAQ VGAHVASPVR FASMIEAMHD AGARVFIEVG
PGATLTSLVG SILGGRSHLA VACDPSGRPG VPGLLHALAR LFVAGLPLHL EPLTAGRTAT
ILDRVTFVPG SNPAAIKAST WLVNGSRARP ANGPEPKRLG PGPALPLPEP GLNPVHATPS
SNGNGNGPLP SPSKNGKKAP EIVMPPPVRS NPPVADQGRE RVLEAFQKTM QMFLEVQRET
MLGFLGTPSG GTPSQAAIRP SHENLASPAP NGQSAPQPPA VPSEAVQPAS AKVSTEVRPE
PVVPTPVPVE SPETSIDVAA RLLSIVQDRT GYPAEMLRLD LDLEADLGID SIKRVEILGT
LREVLPGSGL GSNTDLMDQL SRARTLGAIV EKVERGLKSS QPTLVPAPAS AHTPAQSATN
GHANALSQRS AKNGSLVRRL TLKAVAAPLS RTSGGDLGLA ASGLLLVTDD GRGVSHALAG
ELRSKGHPVV VVGHSSAGSN ESDSDVQSVD LTSPAAVDAL LARLRNQGPL AGIIHALPLQ
HGRSAGLDSQ LWSARMGPES RGLFLLARAG ADDLTRAAEQ GGACLIACTA MGGSFASAGA
ASDDFFPGQG AVAGIVKTLA REWCRAIRVR VVDFDPREEA TTVAANLIHE IEARDRRTEV
GYLDRSRVAL RVVESPLSVA GRSEWQPALG EPILVTGGAR GITAVLTTEM AKCWKPTFLM
VGTTPLPRED ESRLTVGVTN PATLKSLLHQ RLTEEEQGAG LVELERAYQT LRRQREIRSN
LERLRTFGSQ VDYAQVDVRD LEALRTVLAR WQARFGPVRG LIHGAGVIHD KLLRDKTLES
YDRVLGTKLD GALNLASLLD PDSLRFAAFF SSVAGRFGNR GQVDYAAANE TLNKLALWLD
RRWAGRVVSV NWGPWSGVGM VSDLESHLQG QGLGMISPDQ DAHRLTDELR LGRKGEVEVV
IAGEIGSLLD PDEKPSRAGR ELERINEDFV MS
//
