AGDC_ASPTN
ID AGDC_ASPTN Reviewed; 879 AA.
AC Q0CMA7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Probable alpha/beta-glucosidase agdC;
DE EC=3.2.1.20;
DE EC=3.2.1.21;
DE Flags: Precursor;
GN Name=agdC; ORFNames=ATEG_05177;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Has both alpha- and beta-glucosidase activity (By similarity).
CC {ECO:0000250}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476600; EAU34246.1; -; Genomic_DNA.
DR RefSeq; XP_001214355.1; XM_001214355.1.
DR AlphaFoldDB; Q0CMA7; -.
DR SMR; Q0CMA7; -.
DR STRING; 341663.Q0CMA7; -.
DR EnsemblFungi; EAU34246; EAU34246; ATEG_05177.
DR GeneID; 4320812; -.
DR VEuPathDB; FungiDB:ATEG_05177; -.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_0_1; -.
DR OMA; DAYFPDD; -.
DR OrthoDB; 151244at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; IPR030458; Glyco_hydro_31_AS.
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.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..879
FT /note="Probable alpha/beta-glucosidase agdC"
FT /id="PRO_0000394918"
FT REGION 446..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 429
FT /evidence="ECO:0000250"
FT ACT_SITE 580
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 879 AA; 98442 MW; 7D0D7DA1D2763950 CRC64;
MLGSLLLLAP LAGAAVIGSR SNNTEPCPGY KVSNVREGVN SLTADLSLAG KPCNTYGTDL
KDLKLLVEYQ TERPDERLHV MIYDANEQVY QVPESVVPRV EGRKGARPHS ALKFTYEEEP
FSFTVTRDDE VLFDTSASNL IFQSQYLNLR TWLPEDPYLY GLGEHTDSLR LPTTNYTRTI
WNRDSYGVPQ NSNLYGAHPV YYDHRGESGT HGVFLLNSNG MDIRIDKTED GQQYLEYNTL
GGVFDFYFFT GSTPKETSME YSKIVGLPAM QSYWSFGLHQ CRYGYRDVYQ VAEVVYNYSK
AGIPLETMWT DIDYMNARKV FTLDPERFPL PKMRELVDYL HKHDQKYIVM VDPAVSAVDN
EAYEHGVDQG IFLQQQNGSL YKGAVWPGVT VYPDWFHPDI QEYWNSEFSA FFSADDGVDI
DGLWIDMNEA ANFCTWPCAD PEQYAIDNDL PPAPPAVRPS NPRPLPGFPD SFQPSSSKRA
VKRAGGSKGA KVGLPGRNLV DPPYKIQNAA GSISNKTINT DIIHAGEGYA EYDTHNLYGT
MMSSASRGAM LNRRPDVRPL IITRSTFAGA GSHVGHWLGD NLSQWDQYRI SISQIVAFAS
MFQVPMVGAD VCGFGGNTTE ELCARWAALG AFYTFYRNHN EIGSTSQEFY QWPTVADSAR
KAIEIRYKLL DYIYTAFHKQ TETGEPFLQP MFYLYPEDEN TFANDVQFFY GDALLVSPVL
TEGSTSVDAY FPDDIFYDWY TGAPVRGHGA KKTLENIDVT HIPLHVRGGN IIPVRSSGAM
TTKELRNKSF ELIIAPGLDG TASGSLYLDD GDSLEQKGTA EIKFEYRRGK LSVKGSFGRS
AAGVKVQAVK VLGQKAESRM SAFRSTEFEL TRPMEISLQ
