AGDC_EMENI
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 25-MAY-2022, entry version 93.
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; 162425.CADANIAP00000088; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR CLAE; AGL31C_EMENI; -.
DR EnsemblFungi; CBF78576; CBF78576; ANIA_07345.
DR EnsemblFungi; EAA61716; EAA61716; AN7345.2.
DR GeneID; 2869771; -.
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; VWPDFTH; -.
DR OrthoDB; 151244at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 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
