ID   MANBA_ASPCL             Reviewed;         932 AA.
AC   A1CTM5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=ACLA_083570;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06662.1; -; Genomic_DNA.
DR   RefSeq; XP_001268088.1; XM_001268087.1.
DR   AlphaFoldDB; A1CTM5; -.
DR   SMR; A1CTM5; -.
DR   STRING; 344612.A1CTM5; -.
DR   GlyCosmos; A1CTM5; 12 sites, No reported glycans.
DR   EnsemblFungi; EAW06662; EAW06662; ACLA_083570.
DR   GeneID; 4700372; -.
DR   KEGG; act:ACLA_083570; -.
DR   VEuPathDB; FungiDB:ACLA_083570; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_3_0_1; -.
DR   OMA; EFIYFSQ; -.
DR   OrthoDB; 2504097at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000006701; 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; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..932
FT                   /note="Beta-mannosidase A"
FT                   /id="PRO_0000394643"
FT   ACT_SITE        480
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        538
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        609
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        632
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        659
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        739
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        762
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        791
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   932 AA;  104680 MW;  AFDBB74995D092FD CRC64;
     MRIREQTILA LLSPGLPPVT GQHVLDLSEP GWTVSSKALN RTVPGRLPSQ VHLDLFEAGV
     IATMGSMILT FAGLRMPTGR TPATLLLGCE LTDHESTWLV FDGLDTFTTI TFCDQIIGST
     YNQFRQYHFD VSQVLKECKQ EGPVLSINFG SAPNIANAIA NGPSAEEWPA GVQITNEYPN
     RWYIRKEQSD FGWDWGPAFA PAGPWKPAYI VQNKNPDRLY VLNTDLDIYR RGQINHLPPD
     QSQSWVVNAS IDVLGSVPQW PSMSVEIKDA YSGVVLSSGL LENVTVSGNS VTGVTVVDGR
     TPKLWWPNGM GDQSLYNVTI AVHNHRNQVV AEVMKRTGFR TIFLNQRNIT EEQLAQGVAP
     GANWHFEING REFYAKGSNI IPPDAFWPRV TPSRMERLFD AVTAGNQNML RVWASGAYLH
     DFIYDLADEK GILLWSEFQF SDALYPVDDA FLENVAAEVV YNVRRVNHHP SLALWAGGNE
     IESLMLPMVR RADHKGYAKY VGEYEKLYIS LILPLVYENT RSITYSPSST TEGYLHVNLS
     APVPMTERYS NTTPGSYYGD TDYYNYDTSV SFNYHKYPVG RFANEFGFHS MPSLQTWQQA
     VDPKDLYFNS SVVVLRNHHY TAGGLFTDNY QNSSRGMGEM TMGVESYYPI PSKSDPVANF
     SAWCHATQLF QADMYKAQIQ FYRRGSGMPE RQLGSLYWQL EDTWQAPTWA GIEYDGRWKM
     LHYVARDIYE PIIVSPFWNY TTGDLEVYVT SDLWEPAQGT VNLTWVDLSG KSIAGNAGTP
     ESIPFSVGAL NATDVYSANV ADLSPPDLTD SILILSLAGE GYLPNARTRS EFRHENQFTP
     VFPKDLALRD PKLELAYNPD TRTFTVEATA GVSLYTWLDY PAGVVGYFEQ NGFVLLPGMK
     KEIGFVVQEG SVDEDWMRSV TVTSLWDQKV RE
//