ID   MANBA_ASPFC             Reviewed;         926 AA.
AC   B0Y7S2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-MAY-2023, entry version 62.
DE   RecName: Full=Beta-mannosidase A;
DE            EC=3.2.1.25;
DE   AltName: Full=Mannanase A;
DE            Short=Mannase A;
DE   Flags: Precursor;
GN   Name=mndA; ORFNames=AFUB_074800;
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 144.89 / FGSC A1163 / CEA10;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC       residue from the non-reducing end of beta-mannosidic oligosaccharides
CC       of various complexity and length. Involved in the degradation of
CC       polymeric mannan and galactomannan (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase A subfamily. {ECO:0000305}.
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DR   EMBL; DS499599; EDP49453.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y7S2; -.
DR   SMR; B0Y7S2; -.
DR   GlyCosmos; B0Y7S2; 15 sites, No reported glycans.
DR   EnsemblFungi; EDP49453; EDP49453; AFUB_074800.
DR   VEuPathDB; FungiDB:AFUB_074800; -.
DR   HOGENOM; CLU_005015_3_0_1; -.
DR   PhylomeDB; B0Y7S2; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000001699; 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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..926
FT                   /note="Beta-mannosidase A"
FT                   /id="PRO_0000394644"
FT   ACT_SITE        474
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        311
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        532
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        603
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        626
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        653
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        733
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        756
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        785
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        819
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        905
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   926 AA;  103736 MW;  0926E59CD2AE6E7A CRC64;
     MHVKAETVLA LLTPAPPSVV GQHVVDLSGD GWTLSSTALN RTVPGHLPSQ VHLDLFEAGV
     IDIMASMILT FVGLRMPIGR IPATRLKAYF ESTWLVFDGL DTFATITFCD QHVGSTDNQF
     RQHHFDVSQI LKECKQDPVL RINFGSAPNI ANTIAKSPDA EEWPPGVQIT NEYPNRWYIR
     KEQSDFGWDW GPAFAPVGPW KPSYIVQNSH AELYVLNTDI DIYRQGQINY LPPDQSQPWI
     VNASIDFLGP VPCKPSMSIE IKDAATGSVL SSGLLQNVTV SGKSITGTTT IDGDAPKLWW
     PSGMGKQNLY NVTITVQNDM KKSLAKVTKR TGFRTIFLNQ RNITDDQLAQ GIAPGANWHF
     EINGYEFYAK GSNIIPPDAF WPRVTQARMA RLFDAVTAGN QNMLRVWASG AYLHDFIYDL
     ADEKGILLWS EFQFSDALYP VNDAFLENVA AEVVYNVRRV NHHPSLALWA GGNEIESLML
     PMARRADPTG YSKYIGEYEK LYISLILPLV YENTRSITYS PSSTTEGYLY VNLSAPVPMA
     ERYSNTTPGS YYGDTDYYNY DTSVSFDYNH YPVGRFANEF GFHSMPSLQT WQQAVDPEDL
     QFNSSVVVLR NHHYTAGGLF TDNFKNSSKG MGEMTMGVEA YYPIPSKSDS VANFSAWCHA
     TQLFQADLYK SQIQFYRRGS GMPERQLGSL YWQLEDIWQA PTWAGIEYDG RWKVLHYVAR
     DIYQPIIVSP FWNYTTGRLE VYVTSDLWEP AQGTVNLTWV DLSGKSIANN AGTPETVSFT
     VGALNTTNIY TTNISELSLP DLKDSILILS LSGEGRLPNA SSKKAFVHQN HFTPVFPKDL
     SLKDPKLEVS YSPESRKFTV QATGGVSLYT WLDYPAGAVG YFEANAFVLL PGVPKEVSFV
     AQEGNVTDDW LQRVTVQSLW DQKVRD
//