ID A0A2H3IX48_WOLCO Unreviewed; 1084 AA.
AC A0A2H3IX48;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=WOLCODRAFT_113536 {ECO:0000313|EMBL:PCH34301.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH34301.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH34301.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH34301.1,
RC ECO:0000313|Proteomes:UP000218811};
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 -!- 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; KB467831; PCH34301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IX48; -.
DR STRING; 742152.A0A2H3IX48; -.
DR OMA; AIQNMEL; -.
DR OrthoDB; 8526at2759; -.
DR Proteomes; UP000218811; 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:UP000218811};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 390..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1084 AA; 117382 MW; 7DA399E107EEB29E CRC64;
MPVSAPPAIP PIEPDIFDDD DEGWQDMPVV RNEDDALGLD EEDQKKYHYV PPAKKAGGGG
NATGNLLDVD YRGNEWRAKV DQNENEYTRL RINEEDESDE VHLRTRYLFD EDKAMTPLSQ
MQATKDLLTE AQRIAYVGLC ALTSREMSDR LKVVNRKELK KAIDDMELWA LKIMGRLHYH
MELSTEEQKM INSLAMHGIQ AKDLAPALMT THTVANPEYD PAEARRQADE QRRSELAQLD
ALESDSADVS ESAPSTPTPP SASNNSVRSK SSTPKPYQTT ARVLENTSES VPGVSTHLSA
ADEKVTLDIR WTVLCDLFLV LIADSVYDAR SRVLLESVAL KLGLGWLDVV KFERRVTEAL
EIEESVEKLE QGEVIQGVQK NTRKRRYMML GLATLGGGLV IGLSAGLLAP VIGAGLGAAF
TTIGITGTTG FLAGTAGAAV ITTGGVLTGS GLAVRGMANR TRYVRTFDIL PLHNNKRVNC
ILTVPGFMTG AHDDVRLPFS VLDPVVGDVF SVLWEPEMIK ETGSALRILT SEVLTQLAQT
ALQATVMTAL MSALQWPIIL TKLGYLIDNP WSNALDRAKA AGLVLADVLL QRHLGVRPIT
LIGFSLGARV IFYALVELAK HKAFGIVQDV FLLGATVTAP LRTWLEVRSV ISGRFVNGYA
RNDWVLNYLF RATSGGLNTV AGLRAVENVP GLENVDVTDK IAGHMSYRTF MPLILDQLGF
PVSADYFDEP VEPDFEEDRI VVREGEENSK KRGWFLRRKK SSNPVSRVSR PPSAASFSFQ
KKERTSLSSI ADDELPPREG AASSSPAPTP HAAAPTSQTA SADASHPDTS ADAPDGDVAN
SQIPMHAGFN FDAIKDVIGK AELNPAETQI PAPSQTPASH VHEPIQRTGS VPLPAPNSPE
ATPTMRSSLD LRPAEEEDPI AGPSSYTRSD LISRTKSLNL LPNTTHESVD DQSSLYSRAR
PAAFNAGGSP WPTEEPDATP TFGGFGGYRD ALRSQETLSF GSSGGSSLAP PTFGSYSSSA
SAHESIFSQP HDATLSFGGA DGSITLSPSP LTMERDPWAI TARTFSGEGS KKSTSTLDLN
PWQS
//
