ID S3E4N1_GLAL2 Unreviewed; 927 AA.
AC S3E4N1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Beta-mannosidase A {ECO:0000256|ARBA:ARBA00021795};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Mannanase A {ECO:0000256|ARBA:ARBA00031061};
GN ORFNames=GLAREA_06375 {ECO:0000313|EMBL:EPE33363.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE33363.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE33363.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000829};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000256|ARBA:ARBA00004740}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC mannosidase A subfamily. {ECO:0000256|ARBA:ARBA00007483}.
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DR EMBL; KE145358; EPE33363.1; -; Genomic_DNA.
DR RefSeq; XP_008079980.1; XM_008081789.1.
DR AlphaFoldDB; S3E4N1; -.
DR STRING; 1116229.S3E4N1; -.
DR GeneID; 19465429; -.
DR KEGG; glz:GLAREA_06375; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_3_0_1; -.
DR OMA; EFIYFSQ; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041447; Mannosidase_ig.
DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF5; BETA-MANNOSIDASE A; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EPE33363.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..927
FT /note="Beta-mannosidase A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004520012"
FT DOMAIN 251..342
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 745..818
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 844..924
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 927 AA; 103610 MW; 2A78216C1C6DCA5C CRC64;
MGVLHRLQVP LVALLSYTAI AQKVIDLGTK QWTLSSPVYN ISVPGRVPSQ VHLDLFREGV
IPDPYVGLGD FELRWVTLTN WTYETTLDGL DSTIPTWLLF NGLDTFTSIE VCGQHVASTN
NQFRQYYFEI SDILKSCSTT PDLSINFGSA VNITADIASE PGQEVWPPGQ VFWPGGVEGV
FEFPNRQFMR KEQSDFGWDW GPAFAPAGVW QPAYVVQLPG PAVHVRNTLL DIYRQGQLNN
LPPDQNAPWI VNASIDVIGS LPSNAKLFIE IMDIKNVTVA SGAMQNMTSI GSTITGSVVV
DGETCQLWWP VGLGPQNLYY FKITVMNGNE SLVSITKRSG FRTIVLNMTP ISESQLAQGI
APGNNWHFEI NGQEFYAKGS NFIPPDAFWP RVTETKMNQL FQSVVDGNQN MLRVWASGAY
TPDFIYDIAD EMGVLLWSEF EFGDALYPVG VEFLENVRQE AEYNVRRVNH HPSLALWAGG
NELENLELRL AAALDPGNDR WRQEYEQLFL GVLLPTVFAN SKSISYIPSS TTNGYLELNF
SLAIPMIQRY DNATKGSIYG DTDHYDYNSL NAFDLSTYPV GRFANEFGFH SMPSLQSWQQ
VLSPEDLHFN STTIVLRNHH YPAGGPLTDN FHSPLHGMGE MTLAAQRYYP VPNMADPVAN
FSAWCQTTQI FQADFYRSQI TYYRRGSGKK ERQLGSLYWQ LEDIWQAPTW AGIEYDGRWK
FLHYVAKDIY QPVIIASYLN TTDGDLTAYV TSDLWSPATG VATLTWYDYN GTILAPPSSV
PFTVGALNIT QVLQTNTKTI PYDLTKAVLK MNITATGSLP NTNDTKTFKH EFFFHALDLS
KANLQDPGLQ LEYNASTGNF TIEATKAVAA WVWMDIPAGT LANFDGNAFW LVPGEKREVG
VVVKSDGSGG KWVEGVRVRS LWDNTQS
//
