EXG1_ARTBC
ID EXG1_ARTBC Reviewed; 413 AA.
AC D4AJL7;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Probable glucan 1,3-beta-glucosidase ARB_04467 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:P29717};
DE EC=3.2.1.58 {ECO:0000250|UniProtKB:P29717};
DE AltName: Full=Exo-1,3-beta-glucanase {ECO:0000250|UniProtKB:P29717};
DE Flags: Precursor;
GN ORFNames=ARB_04467;
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, SUBCELLULAR LOCATION, AND INDUCTION.
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: Major glucan 1,3-beta-glucosidase required for cell wall
CC integrity (By similarity). Beta-glucanases participate in the
CC metabolism of beta-glucan, the main structural component of the cell
CC wall (By similarity). Can also function biosynthetically as a
CC transglycosylase (By similarity). Functions to deliver glucan from the
CC cell to the extracellular matrix (By similarity). Involved in cell-
CC substrate and cell-cell adhesion (By similarity).
CC {ECO:0000250|UniProtKB:P29717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000250|UniProtKB:P29717};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P29717}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460,
CC ECO:0000269|PubMed:21919205}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:P29717}. Note=Is non-covalently attached to the
CC cell wall. {ECO:0000250|UniProtKB:P29717}.
CC -!- INDUCTION: Expression is down-regulated in presence of human
CC keratinocytes. {ECO:0000269|PubMed:21247460}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; ABSU01000001; EFE36940.1; -; Genomic_DNA.
DR RefSeq; XP_003017585.1; XM_003017539.1.
DR AlphaFoldDB; D4AJL7; -.
DR SMR; D4AJL7; -.
DR STRING; 663331.D4AJL7; -.
DR EnsemblFungi; EFE36940; EFE36940; ARB_04467.
DR GeneID; 9522430; -.
DR KEGG; abe:ARB_04467; -.
DR eggNOG; ENOG502QPYU; Eukaryota.
DR HOGENOM; CLU_004624_0_1_1; -.
DR OMA; DTHHYQV; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..413
FT /note="Probable glucan 1,3-beta-glucosidase ARB_04467"
FT /id="PRO_5003053255"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O85465"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P29717"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29717"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29717"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29717"
FT DISULFID 282..412
FT /evidence="ECO:0000250|UniProtKB:P29717"
SQ SEQUENCE 413 AA; 45416 MW; 4B907FA7CEABEBC7 CRC64;
MKFGSLLGLS LVGLSVASPV TNVWKSPRAA DDFIRGVNLG GWLVLEPWIT PGIFEEGGDS
AVDEWTLSAA LGHRAHERLK LHWNTFMEQK DFDRIKGAGL THVRIPIGYW AVAPIQGEPF
VQGQVDMLDA AIDWARHSGL KVNVDLHGAP GSQNGFDNSG RLGPANWQKG DTVAQTYKAL
DVLIQRYAKK DGVVDEINLI NEPFPQAGIQ VEPLKDYYRQ GAAKVKSANP NVAVVISDAF
MGPSKWNGFD VGAKTIIDTH HYQVFSPQLV AMDINQHVKA ACDFGNDELA KSSIPAIVGE
WCGALTDCTQ YLNGRHEGAR YDGTHKDSDP KTAVPNGCVR KTGGSASQLT DEEKTNTRRY
IEAQLDSFSK GHGWFWWTWK TERGSPGWDL NDLLSNGLFP QPLDSRMFLG QCN
