ID A0A094H3X2_9PEZI Unreviewed; 847 AA.
AC A0A094H3X2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE RecName: Full=Alpha-glucuronidase {ECO:0000256|ARBA:ARBA00012271, ECO:0000256|PIRNR:PIRNR029900};
DE EC=3.2.1.139 {ECO:0000256|ARBA:ARBA00012271, ECO:0000256|PIRNR:PIRNR029900};
GN Name=aguA {ECO:0000256|RuleBase:RU361198};
GN ORFNames=V502_11258 {ECO:0000313|EMBL:KFZ03061.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ03061.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ03061.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Alpha-glucuronidase involved in the hydrolysis of xylan, a
CC major structural heterogeneous polysaccharide found in plant biomass
CC representing the second most abundant polysaccharide in the biosphere,
CC after cellulose. Releases 4-O-methylglucuronic acid from xylan.
CC {ECO:0000256|RuleBase:RU361198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate;
CC Xref=Rhea:RHEA:20005, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:58720, ChEBI:CHEBI:58899; EC=3.2.1.139;
CC Evidence={ECO:0000256|ARBA:ARBA00000762,
CC ECO:0000256|PIRNR:PIRNR029900, ECO:0000256|RuleBase:RU361198};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361198}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family.
CC {ECO:0000256|ARBA:ARBA00008833, ECO:0000256|PIRNR:PIRNR029900,
CC ECO:0000256|RuleBase:RU361198}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ03061.1}.
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DR EMBL; JPKE01004267; KFZ03061.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094H3X2; -.
DR STRING; 1420915.A0A094H3X2; -.
DR HOGENOM; CLU_007125_2_0_1; -.
DR OrthoDB; 2783531at2759; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR037054; A-glucoronidase_C_sf.
DR InterPro; IPR011395; Glyco_hydro_67_aGlcAse.
DR InterPro; IPR005154; Glyco_hydro_67_aGlcAse_N.
DR InterPro; IPR011099; Glyco_hydro_67_C.
DR InterPro; IPR011100; Glyco_hydro_67_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR Pfam; PF07477; Glyco_hydro_67C; 1.
DR Pfam; PF07488; Glyco_hydro_67M; 1.
DR Pfam; PF03648; Glyco_hydro_67N; 1.
DR PIRSF; PIRSF029900; Alpha-glucuronds; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361198};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR029900};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029900};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361198};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000256|PIRNR:PIRNR029900}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..847
FT /note="Alpha-glucuronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013017431"
FT DOMAIN 21..137
FT /note="Alpha glucuronidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03648"
FT DOMAIN 149..470
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 472..694
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
FT ACT_SITE 302
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
FT ACT_SITE 410
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR029900-1"
SQ SEQUENCE 847 AA; 94422 MW; 81656B020450CFCE CRC64;
MRSLLFLLLL GLVAAEDGLD GWLRYAPLPR ASYNHLSFPT SIVALNSSKD SPVYSAGLEL
QKGIKGILSK QIKISHDGKS TSSVIVVGTV DEYVKSSRKS HNAPKLGEDG FWLSIHGNTV
TILGQNERGA LYGAFEYLSR LAQGDFSPAA YATSPDAPIR WVNHWDNLNG TGTHGSVERG
YGGDSIFYKD NVIYQDLSRV TDYARLLASI RINGVVINNV NADPAFLTDE YLEGVARIAN
HFRPYGVKVG LSLNFAAPQL IGGLDTFDPL DPSVIEWWAT ITDKVYQYVP DMAGYLVKAN
SEGQPGPLTY NRTLLDGANL FAKAARPHGG IVMFRAFVYD HLTLNETNWK ADRANAAVEN
FLEFDGQFED NIVVQIKYGP IDFQVREPVS PLFANLPKTN VAIELQVTQE YLGQQCHLVY
LPPLWNTILD FDLRVDNKKT LVRDVLSGKR FKRDLGGYVA VSNVGINSTW LGSHLAMSNL
YAYGRMAWDP TVNAKSTLED WIRLTFGLDR SVIDTISKMS MQSWPAYEQY TGNLGIQTLT
DILYAHYGPN PPSQDDNPWG QWTRADSDSI GMDRTVWNGT GFSGQYPPEV ARMYESINTT
PDELVLWFHH VPYTHRLHSG KTVIQHFYDE HYKGAETAHN FIAMWKSLKG RVDSQRYEEV
LFRLVYQAGH SIVWRDAINN FYNNKSGIAD KLNRVGNHPW RIEAESMVLK SYAPVAVNPF
FTASGFKGIV TTSNTTAGTT TAGTATTKIN FPSGTYDLAV GYYDIIRGKA NWKIYVNDHL
LGSWYGDNED KLGHWPSEFL DGHSATRITF EGVKIKKGDT IKIVGTPDGP ELAPIDYIVL
LPKGIID
//
