ID A0A371D2S0_9APHY Unreviewed; 1083 AA.
AC A0A371D2S0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=OH76DRAFT_1355455 {ECO:0000313|EMBL:RDX46811.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX46811.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX46811.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX46811.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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 TMCO4 family.
CC {ECO:0000256|ARBA:ARBA00009824}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
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DR EMBL; KZ857424; RDX46811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371D2S0; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007941; DUF726.
DR PANTHER; PTHR17920:SF24; LIPASE MIL1-RELATED; 1.
DR PANTHER; PTHR17920; TRANSMEMBRANE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 4 TMCO4; 1.
DR Pfam; PF05277; DUF726; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 389..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 116338 MW; 1FA15B26837AB61F CRC64;
MPVVSAPPIA PIEPDLFDDD DEGWQDMPVV RDDEGFALGL DEEDQKKYHY VARDKKDEAV
TGGAGNATGA LLDVDYKGNE WRTKADQNES EYTRLRMKEE DESDEVHLRT RYLFDEDKAM
TPLSQMQQTK DMLTEAQRIA YVGLCHLTSK EMVDQLKKVN KKELKKAIQN MELWALKIMG
RLYYHMELAT EEQKMIESLG QHGIEAKDLV PPLMTTHTVA NPEYDPAEAR RQAEIREVEA
TEASADISDT SDTTPPSTPP PAYSSVAPPV PPKPQQTTAK VFDDTAAPAM PGVSTHLSAA
DKDVTLDIRW TVLCDLFLIL IADSVYDARS RVLLENVALK LGLGWLDVVK FESRVTEALE
IQEGVEKLEQ QTSIQEAEKS NKKRRYMMLG LATLGGGLVI GLSAGLLAPV IGAGLGAAFT
TIGIGGTTGF LAGTGGAAVI TTGGVLTGSG IAARGMARRT QFVRTFDILP LHNHKRVNCI
LTVSGFMTGA QDDVRLPFSV LDPVVGDVFS VLWEPEMIRE TGSALKILTS EVLSQIAQTA
LQATVMTALM SALQWPIILT KLGYLIDNPW SNALDRAKAA GSVLADVLLQ RHLGVRPITL
IGFSLGARVI FYALLELAKK GAYGIVQDVF LLGTTVTAPL TTWLQVRSVV SGRFVNGYAR
NDWVLNYLFR ATSGGLNTVA GLRPVENVPG LENVDVTDKI SGHMSYRTFM PLILDQLGFP
VSADYFDEPE EPDFEGDRVV IKEGEEKEKR GWFRRKKKTS TTTESISRPP SAATFGIAKK
TTSDSSTADD DDLPPREGTS VPTSSTPVAV QSPSKSPTGA DDGDLGSSEL PAHAGFDFAA
IKEAIGKSDL RPEELQVPQS RFPPLSMPAP TLRTESAPPS IPEPSSPATP RARPSLDLPP
IPSEEGPIAG PSTSPRADLS STLSRSLSLN NMREADEADM TSFGAPSPLL AASRQPVLSF
GGSDSSVWPS QEPDRTPTYA GFGGGYLSTN LSAMRSTDVL ANPFASGSGG LRAGALPSPR
DNPFASAGAP ALSFGGADGS ISILPTTSPS ATPPSRSPWD IGNPYGSGKK PSASTLDLNP
WQS
//
