ID   AGDC_EMENI              Reviewed;         894 AA.
AC   Q5AWI5; C8VCK6; Q1HFR7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Alpha/beta-glucosidase agdC;
DE            EC=3.2.1.20;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=agdC; Synonyms=agdD; ORFNames=AN7345;
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 [MRNA], AND FUNCTION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
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).
RN   [2]
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   [3]
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).
CC   -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC       biomass. Has both alpha- and beta-glucosidase activity.
CC       {ECO:0000269|PubMed:16844780}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA61716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ490507; ABF50883.1; -; mRNA.
DR   EMBL; AACD01000128; EAA61716.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001304; CBF78576.1; -; Genomic_DNA.
DR   RefSeq; XP_680614.1; XM_675522.1.
DR   AlphaFoldDB; Q5AWI5; -.
DR   SMR; Q5AWI5; -.
DR   STRING; 227321.Q5AWI5; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   CLAE; AGL31C_EMENI; -.
DR   GlyCosmos; Q5AWI5; 10 sites, No reported glycans.
DR   EnsemblFungi; CBF78576; CBF78576; ANIA_07345.
DR   KEGG; ani:AN7345.2; -.
DR   VEuPathDB; FungiDB:AN7345; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   HOGENOM; CLU_000631_11_0_1; -.
DR   InParanoid; Q5AWI5; -.
DR   OMA; YICVEND; -.
DR   OrthoDB; 5480935at2759; -.
DR   Proteomes; UP000000560; Chromosome IV.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0015926; F:glucosidase activity; IDA:AspGD.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR   CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF67; ALPHA_BETA-GLUCOSIDASE AGDC-RELATED; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..894
FT                   /note="Alpha/beta-glucosidase agdC"
FT                   /id="PRO_0000394919"
FT   ACT_SITE        429
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        600
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        601
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        802
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   894 AA;  100075 MW;  6AE3AD13A10C594D CRC64;
     MAGTLLSWTP LALALMARAL SQLPLTDCPG YRVINVEERP RGLTADLTLA GTPCNVYGVD
     IENLRLETDY DTNQRLHVKI YDADENVYQV PDSVFPRPVV NDQACADENT PELRFSYAED
     PFSFAVSRAS NDETLFNTTG HNLIFQSQYV NLRTSLPQNP NLYGLGEHSD PLRLNTINYT
     RTLWNRDAYT IPAGTNLYGA HPMYIDHRGE AGTHGVFLLN SNGMDIKIDK NSDNIQFLEY
     NILGGVLDFY FFAGPSPKDV SVQYAEVAGL PAMVPYWGLG FHQCRYGYRD IFEVAAVVHN
     YSEARIPLET MWTDIDYMDH RKVFTLDRER FPLDTVRALV QYLHQRDQHY IVMVDPAVAH
     SENGAFTRGL EKDVFMRKQD GTLYQGAVWP GATVFPDWFH PNTSDYWINE FALFFNAESG
     VDIDALWIDM NEAANFCDWP CTDPVAYAEE NNLPPEPPAV RPNPSSLPGF PAEFQPVNSN
     NNNSSRKRET QVVIAARQGF VKVGNDNGNG RRLGLQGREL IDPPYKIANA AGSLSNKTMN
     TDIFHANGLA EYDTHNLYGT MMSSLSRDAM LYRRPEKRPL VITRSTFAGA GSYVGHWLGD
     NASTWTKYRI SIAQMLAFAS IFQIPMVGSD ACGFTGNTTE ELCSRWATLA AFNPFFRNHN
     EYGMVSQEFY RWNSVAEAAR KAISIRYSLL DYLYTEFHEQ TVTGEPFLLP LFFVYPNDPN
     VVGIDSQFFY GDAILVSPVI EEGKTEVHAY FPGDLFYDWY TGLPLRGNGE VITLTDIGYT
     DIPLHVRGGK IVPVRTGSAG MNTTTEVRKS GFRLVIAPGL DGRAAGRLYI DDGESLEQTA
     MVDVVFTYED GRVSVDGVFT LQTDLRVEAV TVFGDNVVER TIDLPLSGPG GVEL
//