ID R7SS30_DICSQ Unreviewed; 1718 AA.
AC R7SS30;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=(4-O-methyl)-D-glucuronate--lignin esterase {ECO:0000256|ARBA:ARBA00026105};
DE EC=3.1.1.117 {ECO:0000256|ARBA:ARBA00026105};
GN Name=pks1 {ECO:0000313|EMBL:EJF58999.1};
GN ORFNames=DICSQDRAFT_148781 {ECO:0000313|EMBL:EJF58999.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF58999.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF58999.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF58999.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-
CC O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+);
CC Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668;
CC EC=3.1.1.117; Evidence={ECO:0000256|ARBA:ARBA00024511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000256|ARBA:ARBA00024511};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
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DR EMBL; JH719429; EJF58999.1; -; Genomic_DNA.
DR RefSeq; XP_007368302.1; XM_007368240.1.
DR SMR; R7SS30; -.
DR GeneID; 18836771; -.
DR KEGG; dsq:DICSQDRAFT_148781; -.
DR HOGENOM; CLU_000022_6_4_1; -.
DR OMA; GQCRPWD; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000053319; Unassembled WGS sequence.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
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 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1259..1336
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 50..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1718 AA; 186561 MW; 7C792E927B9FD55C CRC64;
MSRICPPSSH NQSRSIAIVG MASTFPNAPN PEVLWDVLLG GQITVAEVPP ERFSLSEQQE
GDAESSRDPH TLRGNFIDQP DIFDNAFFHV SPREAQSMDP QQRLLLHVAY HALENAGYIP
NATRSWNPET FGTFVGVATN DYVHNLRSNI DVYYSTGTLQ SFLSGKIAYT FGFGGPALVL
DTACSSSIVA IHQACRALQN GDCNAALAGG VNVITSPDMY LGLSRGHLLS ETGQCRPWDA
SADGYGRSEG CGLFVLKRLD DAVADNDRIL VVIRGAEVNQ SGNARSITHP HIPTQVALFE
RLVASTGVHP NDISVAECHG TGTAAGDPAE LEAVRKVFAV GRAPDNPLHI TSVKANIGHA
EAASGAASLA KLILMFRENL IPHHPSFERL NPQIPDLSVD NVRIDTTNVP WTSEGQRLAL
LNNFGASGSN AALILEEYVA SPRPQNVSLR TGAVVGLACK SSAATEKMRD AYIAQLEASE
GDATALHDFA YSATARRQLH PFRIAVGGTS TCEILQALRD APVVQVLPAQ RVVFVFSGQG
SQYDGMAAEL YRELELVSRI VDGCDRKLIE WGFVGILDVF RAPQPAQRSH DPRHIQATQV
ALFVLEYALA QLWISWGVRP VAVVSHSFGE FVALVVAGVM TLDDGLRLVA TRARLVYEKC
TPGETGMTGV HASTEQLEPL LATLSGLEIC CYNGTSHNTV GGPLAELQQL ESLCNDRGYQ
FRRLDIALAY HSAAMDPVLD DLREAVKGIK LKPPQIAVHS NVHGTLVYPG ATIAYSADYF
ARHCREPARF SAGIVDFQAR FCPSDIAAFI EVGPQPTTLS FLRNLQQEGA PLLLPSLRKN
ASDIGVLCST LAKLYCTSVP VQWSKVFTNL APEARLVDLP PYPFADTRFW TPYEERRSAV
VAAAGSPNQQ WDASSMDETS QASASEVSLD DLAELIQGHE VAGFSLCPAS VYADLVLSGA
KRELRRHSRE MMEDVIDLVD VSFPAALVYV PDRPRRLLVN IDIDVSQKYA GSFSITSIDV
HGGDAQTHCS GVLKRTTLST RNSKFLCARG LIERETKRIL AAPAAETFST RTVYDLLFPQ
VVRYSETYRA IQAITVDGES LTAYAICRLP KAKRVRRPPQ ASVVNSVFVD TLFHVAGFLV
NFTSGMNCRD AFICSRVDRV KVLPDLIDPS ASYGVYASAV RLDDAHVVVD VYAVAVESPE
KAVVANLKRV HFRRVALTGF TKMLALTSDR PMDDALIADA DVGSMISTAG RSPAPIEGDA
LHACVRRVIS ETSNITLADI SPEAELSKLG IDSLMTWEIV ARLRSLLPTS SRRLDPLLFA
NATTVDDLIR VVSDHCDTGE APSAIAVRAS LDSSSTLNEE SSWNEDSSGE PVSAKTIGPE
IVKGLGSNAP DLPQLDLVEN AGELVDRPEA IMSLESRSDI KPGSGGDVRY SIWRLQDPNR
TLPPSSCGLL RTNVRTAPFL SLESRTGTTP LFLVHDGTGL IGGYSKLAPL GREVWAIRNH
SFADTYAQYS VCDSERELNT LVNAYLAMLT RNFFDGELGL GGECLMGGWS FGGVVAFELA
QSLLRMGINV KGLILIDAPA PQTSSPFPDA LIDSVVERMD PAHRIAEHLK AQMKRATRTL
VAHDPCLSTR NLRRIPAVYL RSQEGMDITL CDAEVDSRVQ AFLNKENDTW TIPQWKTALG
GEMEVLDIPG DHLSVFDQRN VDEVSEQLRK AIQILLST
//
