ID A0A060SHP9_PYCCI Unreviewed; 1835 AA.
AC A0A060SHP9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=BN946_scf185016.g72 {ECO:0000313|EMBL:CDO73915.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO73915.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO73915.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO73915.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
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:CDO73915.1}.
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DR EMBL; CCBP010000124; CDO73915.1; -; Genomic_DNA.
DR STRING; 5643.A0A060SHP9; -.
DR HOGENOM; CLU_000022_6_4_1; -.
DR OMA; GQCRPWD; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000029665; 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 GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
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; 2.
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; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR020802; PKS_thioesterase.
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:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 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 SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
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; 2.
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:UP000029665};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..459
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1305..1387
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1426..1503
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1835 AA; 199548 MW; F2ECE27580C369EB CRC64;
MLATSSGSEG SMFPQRSQSD RLAPSTDIPT RFPPHSVAVV GMAVDFPGAT STDGLWNILR
DGLNTVQKVP AHRFDVHTFT EASEDTARSM PISKGNFVQD PDAFDNAFFH ISPREARSMD
PQQRVLLRTA YHALEDAGYT PGATPAFDSE TFATFVGVAT EDYVHNLRDN IDVYYSTGTL
RAFLSGRISY AFGFEGPSIV LDTACSSSMV AFHQACRALM AGDCNAALAG GVNIITSPDM
YRGLARGHFL SNAGQCRPWD ASADGYCRAE GCGLFVLKRL EDAITENDRI HAVIRGVEVN
QSGQARSITH PHIPAQVALF EKLVSSADVH PHDVNVVECH GTGTQAGDPA ELEAVRKVFA
VDRAQDNPLH ITSIKANIGH AEAASGAASL AKLILMIRER TVPRHISYQR LNPRIPDLAI
DNVRIDTTAV PWDRRGDKRL ALLTNFGAAG SNGAMIVQEY AVPHRQSAVQ QVMVVGLSCK
TAAAAEQRRR DMLSRLEVNA DDAVSLQDFA YSATARRQLH EYRLAVSGSG KEALLTALRP
ARVVRVRPAN QVVFVFSGQG SHCMGMGGDF YRHIPLFTRI VDECHSQLVA NGDPGILTVF
QRATESASSP FDSMRFRTTQ AALFVLEYAL ARVWMSWGVE PSAVVGHSFG EFAALTIAGV
LSLHDALRMV ARRAEIISVR CEPLKTGMTS VRSPPDKLVP MLGRHSFAHL EVCCYNSPSN
FVVGGALDEL QAFEELCVSQ DVRCTRLDVP FAYHSAAMAP ALLELQALSG SLVVLPPNIP
VLSNVTGTLI EPGDVSAFSP DYFVRHCREP ARFQQGIASL ASQFDISSTA AIIEVGPHPT
TVPLLRTLQA DGAPLLLPSL RKGSEGMETM CAALAQLYCT DAPVKWRKVF EDLAPGARVV
DLPAYPFAKT RFWVPYEDGP PGRANGPADS KATATGGPAA RPCFSLLDRC VPSSRESEHT
VVAFETDVES LAELIQGHQV AEVPLCPASV YAELALAAGM TVSEARSSSG AENVLELADI
VFSKPFVYIP ERQGRLRIHL TFPEAHGKYW CTFSIRPFDE SRAKSIVYCK GSLKKTTQEK
LLSKFSYSET MVKRDLRTHL EPRSADSTLE TFRTRTVYDL LFPSIVSYSE TYRTIKSISV
NASTSGAYAV IQLSAAILSQ PFATIHPVFV DTLFHVAGFL VNFMCAMNGT DAYICSSVDR
LQLIPDAIDC KAQHGVYATV VKVEDSQGAP SVKRGEVVVV DVYAIEVDGP RERIVARMKR
VRFQKVSLDA FKEALRRAAG TPSARAEVAR VADTALATEA PEDRDGQLLR TGDILNVVAE
TTGIPCDDLT LDARLTHLGI DSLMLWEVAT RLTPLGPARA GQRGLEARDL AEAATLGDLV
ALVRDTLGKR TSLDETSAEN SFTTLCEDIP SRADIASPVP TEERRCLQPI DIQAVRNVLS
SVLDTPVDEI SNTTELGHLG LDSLTSIEAK NALRARLNVE VDQEALFGCR TVQDVYALVA
QDWVVEAAGS REVKENREQP GEARSVHEQA GILSPPFVVS CPGGFHLVRL QSAQKDGVAK
RPLILIHDGS GSVASYARLA PLGRDVWAIR NRNLLEHLLG VGARYEDLVP FLAGSYAKVL
ANLVERCICS EGYYLGGWSF GGVVAFELVK QLERLGVPVK GLILIDAPAP QTQSPLPDWL
INNLVTRILG PSSSTRAAHT DDVQVEWKQA EELAIQMRVS TRALVAYNPE LRDMPTTRPT
GVRVFYLRAT DAVDEEMLSA SGGEELPERV RAFLTKRGDD WTMSQWAKAL GAPNVEVAEV
PGDHFSMFDY ANTQNLSGHV QEAIRVWSEE KAPSA
//
