ID A0A0S2DHB6_LYSEN Unreviewed; 3563 AA.
AC A0A0S2DHB6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Beta-ketoacyl synthase/short chain dehydrogenase/methyltransferase domain {ECO:0000313|EMBL:ALN57844.1};
GN ORFNames=GLE_2495 {ECO:0000313|EMBL:ALN57844.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN57844.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN57844.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN57844.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) 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; CP013140; ALN57844.1; -; Genomic_DNA.
DR STRING; 69.GLE_2495; -.
DR KEGG; lez:GLE_2495; -.
DR PATRIC; fig|69.6.peg.2458; -.
DR OMA; ESMVACE; -.
DR OrthoDB; 9030879at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000061569; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 1.10.1240.100; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 4.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR013217; Methyltransf_12.
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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 4.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 4.
DR SMART; SM01294; PKS_PP_betabranch; 4.
DR SUPFAM; SSF47336; ACP-like; 4.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 3: Inferred from homology;
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 Methyltransferase {ECO:0000313|EMBL:ALN57844.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000061569};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALN57844.1}.
FT DOMAIN 58..481
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1181..1258
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1320..1738
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3187..3265
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3327..3401
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3454..3531
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2250..2305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3293..3314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3406..3459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3533..3563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3406..3430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3563 AA; 376763 MW; A7A1104909B1981C CRC64;
MDSMNRQDVL RDLQSRRITP EQAKRLLAEA AAQPAPAAPS AAAASTARTG ASPSPGADER
IAIVGMSGRY PGADSLDAFW ELLSQGRSGV RTVPASRWDV ERFYDPRPQQ PGKVYCKWLG
ALDDVECFDP LFFGISPAEA TVMDPQHRVF LQEGYRAFED AGYAPAALDG ARCGVYLGIM
GNEYVGLCRQ AGAGIGEATG NSSSIAAARI AYHLNLKGPA IAVDTACSSS LVATHLACQA
LLAGEIDLAL AGGVTLYLSP ETHVSMCAAG MLSASGRCSA FDDSADGFVP GEGVGTLVLK
RLSDAIAAGD RIHAVVLGSG INQDGRTNGI TAPSAKSQAD LLREVYRRHR IDPASISYVE
AHGTGTRLGD PIEFEALSTV FGEATADLHF CALGSVKSNI GHASAAAGVA GVHKTLLSLR
EKRLVPTLHY SRPNPHVELR GSPFVINTEL REWRVPEASA RRAAVSSFGY SGTNAHLVLE
EWNPAEAHAA PQADAREPQL LLLSARGADE LRAQAQALAR WLQRDAATPL ADVAYTLQVG
RAAFEQRLAF VAADRAEALA RLEDFLAGRA APASFAGRVT AQMRESHRAD SAARAPLRAD
ALALAGLGER WVGGFDPDWR DLPRSRPGRF AHLPTYAFAK ERCWVTTGDG ASESGPRSEP
VMQPPAPPVE APVHRVPEAL AALELLIGDT EPVEAPVPQA LDAQARVAIV GASAQAMAQF
ARVWPRATAL APPAADAIGA WADALRALGR IDRLVWFAGD GGGERVDELL DYAARSAPVL
ACFHAIKALL DQGYGDGALE WTLVTRDAGT DPSHAALQGL VASAVKENAQ WSLRLVDLGR
EDAIGAAAGI GVEQLLAVPA DTQGRGWLCH DGQWARERLR PVPVPARTDG AFRRDGVYLI
VGGAGGVGEV FSEYLLRHYQ ARVVWVGRRA ADADIEAKRA RLAALGPAPL YLQADAADPA
ALAAVRAQAL RAYGRIDCVV HSAIELHDQG LAVMDAARFE RAFATKAKIA ANLLGAFADD
AADGVVLFSS LVSYSRDAGQ SNYSAGSLYQ DALARGLASR YGRRVKTLNW GFWGDIGATA
SLPPRVRERF AQAGIGALRP VEAMAALEVF MHAALPQLAA LHRLGAQGLR VPAPEPAADA
AAAQPPAPQA ERAPPIERDA ELAASEPRPD YEPDQTVAAI DLEAHVKHTL LAQLAAILKL
APERIDPDSA FAGYGVDSIS SVRIVRALND ALGIELAGTS LFDHSSVNKL VRHVLQDHDT
AQLQAAVRAA LPQPVAAPAA SAQPATDTDR RATPAANDAS ADSDARAQPA AQRSGAAAAP
GPIAIVGMSG RFPQSPDLQT LWAHLAAGDE VTEPITRWRI DSLGLPDDIK VCPRGGFLGD
IDQFDPLFFN ISGTEANFMD PQHRVLLETS WHALEDAGYA GQGIAGARCG VYMGFNGGDY
GELLHGQPSL PPHAMWGNAA SVLSARIAYY LDLQGPAITL DTACSSSLVA VHLACQGLWT
GETDVALAGG VWIQCTPGFL ISSSRAGMLS PTGRCRAFGD QADGFVPSEG VGVVVLKRLQ
DALDAGDHIY GVIRGSAINQ DGASNGITAP SAGAQERLQR HVYDSFGIDA GRLQMVEAHG
TGTILGDPIE AAALSRSLSH YSDRTGFCAI GSIKTNIGHT GAAAGVAGLI KVLLSLQHRQ
IPPSLHFDRP NPHIAFADSP LTVNTQLKHW EAPAAGRRLA AVSSFGLSGT NAHVVVEEAP
PAAAAASAAQ PTLLVLSGFR EEDLPAQVAA LAEHLERESA LELSAAGYTL AVGRRHHRHR
LALVAHDAAD AAAELRRWLA GGSSRVLAGT ATAGNGGDER FAPARQRLHA LVQARDDGER
ARLLAELAAL HVQGLAPELG SAFASQRRVA LPLYRFSRKR HWVPERAQPR VEAAAAPVAA
VVAPAAVEPA AVVPATVAPA ASAAPATAAP PSAVSPAPKP AAANVAGVVA TAAPLHPFVH
AAIAGADGPR YATRWSGQEP FLRDHVVQGA PMLPGAACLE MARAAAELAR PGQRARQLRN
VVWLRPLAVA EPVDLQVALE PVPARDNELA FRILGAGSDT PHCQGRVVLD AAPGRGSFVD
VGTLRMRCDL RTLKGGDYYR VFDLMGLAYG ESYRGIERAF VGENQLLAQI RLPAAAVQDG
FHLHPSLLDS ALQASIGFEI GDGREERPSD GAAPRSLMLF ALDQIELYGP CTEQMWVWIR
RDPRGNGNKL DIDLCEPTGR VVAALRGVTS REAGAPQRPA AAASASAATR PAQAAPPQPA
PSAPAPVAAP ASAGAHGEAF PGGDRVGALT LAPAWEPAAP PQAEAWPQEK ANVVVIGGDE
TQFAQLRKRH PRARHLPAAI ADTADRAAEE LRGAGNIEHL FWLAPPSQAR AVDSESIVVD
QQRGVMATFR LVKALLKLGY AGKPLGLTVV TVGSQPVADG EPLDPTHAGV HGLIGTLAKE
YPDWRVRLVD VQAGQPWPLD ALLALPADRD GNAWAHRHGR WHRQRWIQCA LPEPEQTAFR
RNGVYVVVGG AGGIGEAFSE YLIRRYAAQV VWIGLRKRDE IVEEKIGRLS QLGPAPHYVS
ADATDQPSLE RACADIERRF GTVHGVVHAA LLMAGDPLER MDEQRFWRGL AAKIEVSVRM
AQAFAHLPLD FVLFFSSIQA LEKTPRQANY AAGCTVEDAY AALLAQQWRC PVRVVNWGYW
GSVGFAAISS GYRNWIAQAG MGSVEPAEGM AALERLLAGP LRQFAFLKTR REDALTGVQF
SDDRLWRVGA TAPVVPLDAP VDLDPAGLAG QGLPARFEGL LLELLRHELD ALGVFAAATA
QAREALIAPQ YRAWLRHTLD LLAEHGLAVR RGEAWHAAGP ASASSPWQEW ERNAPQWLDS
AELAAPVRLA EATLRELGPV LTGQRAATDV LFPKSSPHLV EGIYRDSPVP DYFNKVLCSA
VVRYIERRRR IDPDVRLRIL EIGAGTGGTT APLVRALEPY AACVAEYRFT DISRSFALAA
QDEYAQRAPY MSYGSFDVER AAAAQGIDVG GFDIVVAANV LHATGDIART LRNAKAALKR
NGLLVLNEVC ATSLFAHVTF GLLKGWWLYE DAHLRIPGSP ALSPESWRAV LAEQGFGAIG
LPAEGARSLG QQIVLASSDG WIRQPVGAQV VAVQAGEASR APEPVVAAQA RPVAESAPVA
PAAPAAEDEE AAIRRIVRDA LIATLDVPAH ELRDDAPLTD YGLDSMLAVQ TVEVLNTTAG
TELTTTSLFD HPSIDAVVDH LLSLRPRNAS VAASVANEPA NAVASRAAPP AVAPVAAPQP
QPQPQPQPAV QAPSLMPAPV APAAASAGIA QAIAQALVEI AGIDSGDIRG DAEFVDYGID
SMLAVQIVEA LNRRLVVELT TTSLFDYPTI DALVAHLLAS ASHGAVAAQP SQPSQPSQPQ
ASQSWTPSAP QSQPAPQPQL APQAAVAAPA PQPARSGGLR ERVRQELLAV LAIDAADFDP
ATPFTDYGMD SMLAVQWVER LNQSLRLELT TTTPFDHPTL DALMQHIGEE HAEDAAAATG
ESVAPTPQTA PAKRREQPMS YTI
//