ID K5WLC2_PHACS Unreviewed; 578 AA.
AC K5WLC2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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_212992 {ECO:0000313|EMBL:EKM51092.1};
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:EKM51092.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM51092.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51092.1,
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}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; JH930477; EKM51092.1; -; Genomic_DNA.
DR RefSeq; XP_007400249.1; XM_007400187.1.
DR AlphaFoldDB; K5WLC2; -.
DR GeneID; 18913314; -.
DR KEGG; pco:PHACADRAFT_212992; -.
DR HOGENOM; CLU_013364_5_2_1; -.
DR InParanoid; K5WLC2; -.
DR OrthoDB; 50200at2759; -.
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; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..578
FT /note="(4-O-methyl)-D-glucuronate--lignin esterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003889514"
FT DOMAIN 433..529
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 578 AA; 61333 MW; 8EDEA7C44F94D5B4 CRC64;
MRFFTSSHSR PVALLLCLSG FTQARSLAKR DDTFDWTNLT ASPNLTLTPC YGNLQCARLT
VPLQYSDPSA GEAQVAIVVL PSNLSHDDSA YLGPLLFNPG GPGISGVDSV VEDAALFREI
LGPQYDIVGF DPRGVGHTTP VISLFQSPAE ALEFFAPYPQ NANESISSLG RIVAQAQILG
DLANARAKTV VESVSTPTVA TDMLTITRAF GRDKLSYYGI SYGSLLGATF AAMFPDQVGR
LVIDGIINAH DWYQGTYFAK DSLLDTDAAL ESVYEACVAA GPSLCPIFEN STDLVRARVN
QLISNIHLAP VALFNSSGTT GNVFGVVDYT VVVQQLLGML DSPYTDALGF MQAVVQLEQG
DGTLMFQGTD TQNIDMLATC TFDSSEPFSV GFIDVEGAIE CGDSIVDTRR TLEAARAEYE
SMLEMSSLAT AWYPLTQGIC AGWSIRGKDH LNGSFETNTS FPLLLIGNTF DPATPIENAH
NMSAGFVGSV VLQQNSTGHT SQSGLSTCTG LAVNAYFNNG TLPHSGTVCQ IEAEIFGPPA
GGSSNVSLAA RGQGLGVSAR ALMRKKVTSR STFGGRAT
//
