ID K5WFE8_PHACS Unreviewed; 537 AA.
AC K5WFE8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=PHACADRAFT_206866 {ECO:0000313|EMBL:EKM58025.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM58025.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM58025.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM58025.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(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 carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
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DR EMBL; JH930470; EKM58025.1; -; Genomic_DNA.
DR RefSeq; XP_007393355.1; XM_007393293.1.
DR AlphaFoldDB; K5WFE8; -.
DR STRING; 650164.K5WFE8; -.
DR GeneID; 18912555; -.
DR KEGG; pco:PHACADRAFT_206866; -.
DR HOGENOM; CLU_019364_3_0_1; -.
DR InParanoid; K5WFE8; -.
DR OrthoDB; 1697614at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT DOMAIN 166..387
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
SQ SEQUENCE 537 AA; 60834 MW; 980DF91268E342E9 CRC64;
MGRTKETVPP HLEEMPYAKE PLKTAYVVQR LLTTLLLVPW WAMYYTVQPR RKPRESWGIK
QVISVKFTRR VYRVTELAGV TWGTRNPEKA CKDRELKETR FEWADLLPEQ FRSGIIVDDE
VPFKRVGAFV WPREMPKELN QEPKREPKQD THIDLEAGGK QHIVAIFLHG GGYCHMSAHE
KSSTSKIPRR LVKDKAFDEI YAVEYRLLQH APFPAAVQDA AAVYAHVLRK YQCLPDLDEL
SRHHRPFISR RGRLHPNDAY LEPWGNSRAE LLGTPNLVNT YLKKSCKVVL IGDSAGGNLV
LALARWIRDE GKLPPPDGLL LLSPSCDPSH AFPDTPSSYI PRPHESTDYL VDTPEPRALL
QRTFLGHHPL EMMHSPYVSP ASHRVLRTFY GEVFATSVQD LTIDALTGDF MDKLRTIASV
PPSPDPGTVL GPGMPTPVTP GMELSPSLSH PVIASPRGLS LFSEFPRTCV VLGDAERLER
EVMKLIGAME SDGVRVHTIR VRDAPHDVLM MGWWDEKVRD ETWQSVGRWV AELATSR
//
