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Database: UniProt
Entry: K5V3U0_PHACS
LinkDB: K5V3U0_PHACS
Original site: K5V3U0_PHACS 
ID   K5V3U0_PHACS            Unreviewed;       488 AA.
AC   K5V3U0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
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_160751 {ECO:0000313|EMBL:EKM57251.1};
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:EKM57251.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM57251.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM57251.1,
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 S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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DR   EMBL; JH930471; EKM57251.1; -; Genomic_DNA.
DR   RefSeq; XP_007395069.1; XM_007395007.1.
DR   AlphaFoldDB; K5V3U0; -.
DR   GeneID; 18909172; -.
DR   KEGG; pco:PHACADRAFT_160751; -.
DR   HOGENOM; CLU_008523_10_3_1; -.
DR   InParanoid; K5V3U0; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   PANTHER; PTHR11802:SF64; CARBOXYPEPTIDASE 2-RELATED; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
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..488
FT                   /note="(4-O-methyl)-D-glucuronate--lignin esterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003884448"
SQ   SEQUENCE   488 AA;  53461 MW;  32C99EA8BF9D543A CRC64;
     MARFSRSLKL ALLGLAFVVV GTVGVVVDAV NHVRSTSTPS LNFETFTSEA QPDVGLRFIR
     NSGVCETTPG VDQLSGYIDF GANMSMWFWF FESRHEPETA PFTLWLNGGP GCSSMIGLFQ
     EHGPCHVLED GETTVLNPFS WNNITNIIYV DQPIGTGFSH GTIDVNSTFA SAPAFWSAFQ
     VLLESQEFAK YESREFIFAT ESYGGHYGPE FVTFFDEQNT KIDQGSVNGE KINVSRLMIN
     NGWYDPLLQN EAYVTFATNA PGYGQLQNDS VIAALNQAFF GSGGCQEQEL ACYAAGNGTN
     SNEVCMQADN FCIDNVFVPA VGDRDSDDLR QNSSALFPSE SYVTFLRNAT IMELIGAETR
     YTECSNPVDI QFSKTGDDAR TLLPQLGALV SSGLKTLIWA GDADINCNWL GGHASVLAMD
     WFGNETLHRT PFTNITIRGQ PVAAVQNVDS FSFARVYQAG HEIPAFQPEA AFEIFSQVVR
     GEQLHSVS
//
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