ID A0A165PEW5_9APHY Unreviewed; 550 AA.
AC A0A165PEW5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=DAEQUDRAFT_751384 {ECO:0000313|EMBL:KZT68123.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT68123.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT68123.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT68123.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429069; KZT68123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165PEW5; -.
DR STRING; 1314783.A0A165PEW5; -.
DR OrthoDB; 8526at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007941; DUF726.
DR PANTHER; PTHR17920:SF22; DUF726 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_2G12860); 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:UP000076727};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 183..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 550 AA; 59405 MW; E1634971776C5664 CRC64;
MSDLTKVTSP KELAEAERLA IFEHVFRRLA AHRNTAELYA VAEYTFSTKA QEQKNETKEL
FLKELNGWGQ GLLQHVWLAC QEPGGGPVPE LSPYSDTSLA GLPPLPDKTS VKKVLSTVLL
LHITSRKDYS ARTRAFLFSF TAPDEAAVAG TLKDPTRALE EAERKTKGAK EEASEQSKTL
RRIGIGLGAV AGGVLVGVTG GLAAPLVGAG VSTALGWFGV GGTAAGLLAT GLASSSVVCG
ALFGYYGSRK MADTVGAYLR EVHDLAIMPV RKPRDTLAVR LCISGWLDSQ SDVVAPWTVF
DGDDTFALQW EVQALRDLSN ALTALIKSQT MKYVRAEIIK RTVFASLWAA LSPTVWLNFT
RIIASKTGKV LGKLLEQRVL GNRPISLVGY SLGSLVIFEA LQYLASLPPT RTFHLVQDVY
LFGAPVSTDE AQWTAMRRVV AGRLVNGYGA NDYVLAVLTR LSDVTWNVAG MGPVPIQGVQ
NVECNEVDGH LKWRSMVGES LSKCKAPGIV DKEVAKQVGL EIGIDMDMDE READRIVEQG
RGQASDAEKL
//