ID   AGUA_EMENI              Reviewed;         847 AA.
AC   Q5AQZ4; C8VQN8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Alpha-glucuronidase A;
DE            EC=3.2.1.139 {ECO:0000269|PubMed:16844780};
DE   AltName: Full=Alpha-glucosiduronase A;
DE   Flags: Precursor;
GN   Name=aguA; ORFNames=AN9286;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX   PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA   Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT   "Development and application of a suite of polysaccharide-degrading enzymes
RT   for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
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:0000269|PubMed:16844780}.
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:0000269|PubMed:16844780};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.0. {ECO:0000269|PubMed:16844780};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:16844780};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 67 family. {ECO:0000305}.
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DR   EMBL; AACD01000172; EAA66353.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF87334.1; -; Genomic_DNA.
DR   RefSeq; XP_682555.1; XM_677463.1.
DR   AlphaFoldDB; Q5AQZ4; -.
DR   SMR; Q5AQZ4; -.
DR   STRING; 162425.CADANIAP00001065; -.
DR   CAZy; GH67; Glycoside Hydrolase Family 67.
DR   CLAE; AGU67A_EMENI; -.
DR   EnsemblFungi; CBF87334; CBF87334; ANIA_09286.
DR   EnsemblFungi; EAA66353; EAA66353; AN9286.2.
DR   GeneID; 2867890; -.
DR   KEGG; ani:AN9286.2; -.
DR   VEuPathDB; FungiDB:AN9286; -.
DR   eggNOG; ENOG502QWS4; Eukaryota.
DR   HOGENOM; CLU_007125_2_0_1; -.
DR   InParanoid; Q5AQZ4; -.
DR   OMA; DNNGWGQ; -.
DR   OrthoDB; 127527at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046559; F:alpha-glucuronidase activity; IDA:UniProtKB.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:AspGD.
DR   GO; GO:0045493; P:xylan catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.30.379.10; -; 1.
DR   Gene3D; 3.90.1330.10; -; 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   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; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..847
FT                   /note="Alpha-glucuronidase A"
FT                   /id="PRO_0000393491"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        583
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        689
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        738
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        739
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        769
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   847 AA;  93898 MW;  7532C6CC34FF39CA CRC64;
     MRSFLLLTAL LGVAAVAEDG LAAWLRYAPI PHAKSYHKNL PSVIVPLNAT AGRPIDTAAY
     ELVDGIKGIF GKRVTLKNET RDDPNLPAVT VGTVEAYAEA GGDVSSVPEL IDDGYYLSVA
     GPSVLILGQN ERGALYGTFQ YLERLAQGKV SDTSFASNPS APIRWVNQWD NLQDGGTHGS
     VERGYGGDSI FFWDGRVRDD LTRASQYARL LASIGLNAVI VNNVNANETI LTQENMDGVA
     RIADAFRPYG IQLGLSLNFA SPQSLGGLDT FDPFDERVIS WWGEITDELY ERIPDMAGYL
     VKANSEGQPG PFTYNRTLAD GANLFARALQ PHGGIVLFRA FVYDHENLNE TLDWKADRAN
     AAVEFFDGLD PQFEDNVVIQ IKNGPIDFQV REPVSPLFAH LSQTASAVEL QVTQEYLGQQ
     CHLVYLAPMW KEVLDFDLRV DGKDSVVSDI VSGRRFNNTL GGYAGVVNVG LNTTWLGSHL
     AMSNLYAYGR LAWDPSADSV ELLQEWIKMT FSHDQEVVDV ITKMSMESWP AYENYSGNLG
     IQTLTDILLG HYGPNPASQD GNPWGQWTRA DADSIGMDRT VWNGTGNAGQ YPEEVYQMYE
     NIDTTPDNLL LWFHHVPYTQ RLKSGKTVIQ HFYDAHYRGS ATAQTFVSLW KTIKGKIDKE
     RYEHVLFRLV YQAGHALVWR DSITNFYYNK SGIPDEAGRV GNHPYRIEAE DMELDGYEPY
     LVSPFEAASG SHCIVTSNNS TEGRASTPLK VKNGKYDIAV NYFDQAIGNS TWRLFLDDDL
     VGEWKGDLEY ILGRAPSPYI DGQTAARITF KHVHIKSRST LSIVGIPDGM EPAPIDYVSI
     LPEGVID