ID   MANBA_ASPFN             Reviewed;         914 AA.
AC   B8NP78;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=AFLA_128610;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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}.
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; EQ963481; EED48638.1; -; Genomic_DNA.
DR   RefSeq; XP_002382054.1; XM_002382013.1.
DR   AlphaFoldDB; B8NP78; -.
DR   SMR; B8NP78; -.
DR   STRING; 332952.B8NP78; -.
DR   GlyCosmos; B8NP78; 15 sites, No reported glycans.
DR   EnsemblFungi; EED48638; EED48638; AFLA_128610.
DR   VEuPathDB; FungiDB:AFLA_012680; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_3_0_1; -.
DR   OMA; EFIYFSQ; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000001875; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..914
FT                   /note="Beta-mannosidase A"
FT                   /id="PRO_0000394645"
FT   ACT_SITE        462
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        614
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        641
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        721
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        744
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        773
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        784
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        909
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   914 AA;  102929 MW;  F6DAC075C591E64B CRC64;
     MRFTATAAAL VASSIPATLG QHVRDLSNEK WTLSSDALNH TVPGNLPSHA HLDLLKAGVI
     DDPYHGLNDF NLRWIPESNW TYTTDKIKDL MPIEFCGKYV ASTNNQYRQY SFDVSQILEG
     CNEDPILKID FGSAPNIVNA IAEDRNSPVW PDGIQQTYEY PNRWFMRKEQ SDFGWDWGPA
     FAPAGPWKPA YIVQLPKAQN IHVLNTDLDI YRKGQINHLP PDQSQPWVVN ASIDFVGSLP
     PNPSMSIEFK DTKSGEILTS KRIGNVTVSG NSVTGVTVLG GVTPKLWWPL GLGDQNLYNI
     TVTVTGHQNQ TLAHVTKRTG FRTIFLNQRN ITDAQLAQGI APGANWHFEV NGHEFYAKGS
     NIIPPDAFWP RVTEARMARL FDAVVAGNQN MLRVWSSGIY LHDFIYDLAD ERGILLWSEF
     EFSDALYPVD DAFLDNIAAE VVYNVRRVNH HPSLALWAGG NEIESLMLPT VERKAPEEYA
     KYVGEYEKLY ISLILPLVYQ NTRSITYSPS STTEGYLDVD LSAPVPMVER YHNTTPGSYY
     GDTDFYNYDS SVSFNSHVYP VGRFANEFGY HSMPSLQTWQ QAVDPEDLHF NSTTVMLRNH
     HYPAGGTFTD NFHNTSLGMG EMTIAVQRYY PIPNKLDSVA NFSAWCHATQ LFQADMYKSE
     IQFYRRGSGM PERQLGSLYW QLEDIWQAPS WAGIEYGGRW KVLHYVSRDI YQRIIVSPFW
     NYTTGDLDLY VTSDLWESAK GKVNLTWLDL SGTPLPHNAG TPGSVPFNVG ALNTTKIYST
     NIKNLTLPNP KDAILVLSLS GEGHLPNSDK KTTFTHQNHF TPVFPKDLAL VDPGLELSYN
     TKSKTFTVEA KSGVSLYTWL DYPADVVGYF DENAFVLLPG QKKEIGFTVQ EDNTDGKWVQ
     GVTVQSLWNQ TLEK
//