AGD1_ARTBC
ID AGD1_ARTBC Reviewed; 865 AA.
AC D4B0X3;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Probable alpha/beta-glucosidase ARB_02101 {ECO:0000305};
DE EC=3.2.1.20 {ECO:0000250|UniProtKB:Q5AWI5};
DE EC=3.2.1.21 {ECO:0000250|UniProtKB:Q5AWI5};
DE Flags: Precursor;
GN ORFNames=ARB_02101;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Has both alpha- and beta-glucosidase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q5AWI5}.
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 Evidence={ECO:0000250|UniProtKB:Q5AWI5};
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 Evidence={ECO:0000250|UniProtKB:Q5AWI5};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}.
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; ABSU01000025; EFE30908.1; -; Genomic_DNA.
DR RefSeq; XP_003011548.1; XM_003011502.1.
DR AlphaFoldDB; D4B0X3; -.
DR SMR; D4B0X3; -.
DR STRING; 663331.D4B0X3; -.
DR EnsemblFungi; EFE30908; EFE30908; ARB_02101.
DR GeneID; 9523318; -.
DR KEGG; abe:ARB_02101; -.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_0_1; -.
DR OMA; DAYFPDD; -.
DR Proteomes; UP000008866; 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; 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; 2.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein 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..865
FT /note="Probable alpha/beta-glucosidase ARB_02101"
FT /id="PRO_5003053822"
FT ACT_SITE 428
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9C0Y4"
FT ACT_SITE 431
FT /evidence="ECO:0000250|UniProtKB:Q9C0Y4"
FT ACT_SITE 548
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9C0Y4"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 865 AA; 98088 MW; 7ADF4EBBD795E7D7 CRC64;
MFGRTLALAA VFATTVLSAA ASLEECPGYK VSNVRDNGHT LKADLRLAGK ACNVYGEDIR
QLKLRVEYQT HERLHVIIED SKEDVYQVPE SVFPRPESEE NDSASTKSAL KFSMTQKPFS
FKVTRRATDE VIFDTSNSPL IFESQYLRLR TSLPDEPNLY GLGEHSDPLR LQTEDLVTTL
WNRDAFGIPP GTNLYGSHPV YYDHRGRSGT HGVFLLNSNG MDVKVGSEDG DNGKKYLEYN
ILGGVLDFYF MAGPTPKEVA SQYAEVVGLP AMMPYWGFGL HQCRYGYRDA FNVAEVVYNY
SQAGIPLETM WTDIDYMDGR KVFTLDSKRF PIDEMRALVE YLHDRNQHYI VMVDPAVSYG
DNDAFERGKT QDVFMKSKDG AIYKGAVWPG VTAFPDWFHP GTQDYWNNEF KLFFDPEKGI
DIDALWIDMN EASNFCDWPC SDPEGWERDH DLPPAPPPVR PIPRPLPGFP DKLQPGSVRL
VKRDGTRLRS KAGLPGRDLI DPPYRIQNEA GSISNKTLNT DLVHANGLVE YDTHNLYGTM
LTKYRLGDNL SEWSQYRFSI SQILQFAAIY QVPMVGADVC GFGGNVTEEL CARWAMLGAF
YPFYRNHNDI AGRDQEFYRW ESVTEAARTA IGIRYKLLDY IYTAFHRQTQ SGDPVLNPLF
YIYPEDEDTF AIDLQFFYGD ALLVSPVTEE GATSVEIYLP DDIFYDYYTG EPIEGKGDLI
TMENVPITHI PLHFRGGQIV PMRADSANTT TELRKQPFEL VICLDREGNA EGSLYLDDGD
SLEQPHTSEI NFEYHNGVLK VSGKFDFQNE EALEIKNIFV LGYKQDMNVQ DKGNMNKDSQ
YDARLKKLAI KAKILLTGPS EMTLH
