ID   MANBA_ASPNG             Reviewed;         931 AA.
AC   Q9UUZ3;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-SEP-2023, entry version 87.
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;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=11358516; DOI=10.1046/j.1432-1327.2001.02188.x;
RA   Ademark P., de Vries R.P., Haegglund P., Staalbrand H., Visser J.;
RT   "Cloning and characterization of Aspergillus niger genes encoding an alpha-
RT   galactosidase and a beta-mannosidase involved in galactomannan
RT   degradation.";
RL   Eur. J. Biochem. 268:2982-2990(2001).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 490-504, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, SUBUNIT, AND GLYCOSYLATION.
RC   STRAIN=ATCC 46890;
RX   PubMed=10553664; DOI=10.1016/s0168-1656(99)00172-8;
RA   Ademark P., Lundqvist J., Haegglund P., Tenkanen M., Torto N., Tjerneld F.,
RA   Staalbrand H.;
RT   "Hydrolytic properties of a beta-mannosidase purified from Aspergillus
RT   niger.";
RL   J. Biotechnol. 75:281-289(1999).
RN   [3]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=24021641; DOI=10.1016/j.febslet.2013.08.029;
RA   Reddy S.K., Rosengren A., Klaubauf S., Kulkarni T., Karlsson E.N.,
RA   de Vries R.P., Stalbrand H.;
RT   "Phylogenetic analysis and substrate specificity of GH2 beta-mannosidases
RT   from Aspergillus species.";
RL   FEBS Lett. 587:3444-3449(2013).
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. Releases the terminal mannose
CC       residue from mannobiose and mannotriose, as well as from galactosyl-
CC       mannobiose (GM2), galactosyl-mannotriose (GM3) and di-galactosyl-
CC       mannopentaose (G2M5). {ECO:0000269|PubMed:11358516,
CC       ECO:0000269|PubMed:24021641}.
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:0000269|PubMed:10553664, ECO:0000269|PubMed:11358516};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.3 mM for p-nitrophenyl-beta-mannopyranoside
CC         {ECO:0000269|PubMed:10553664};
CC         Note=kcat is 4048 min(-1) with p-nitrophenyl-beta-mannopyranoside as
CC         substrate.;
CC       pH dependence:
CC         Optimum pH is 2.5-5. {ECO:0000269|PubMed:10553664};
CC       Temperature dependence:
CC         Optimum temperature is 70 degrees Celsius.
CC         {ECO:0000269|PubMed:10553664};
CC   -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC       {ECO:0000250|UniProtKB:O00462}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10553664}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10553664}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10553664}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase A subfamily. {ECO:0000305}.
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DR   EMBL; AJ251874; CAB63902.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UUZ3; -.
DR   SMR; Q9UUZ3; -.
DR   ChEMBL; CHEMBL5417; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   CLAE; MND2A_ASPNG; -.
DR   GlyCosmos; Q9UUZ3; 13 sites, No reported glycans.
DR   VEuPathDB; FungiDB:An11g06540; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1160135; -.
DR   VEuPathDB; FungiDB:ATCC64974_92080; -.
DR   VEuPathDB; FungiDB:M747DRAFT_299830; -.
DR   BioCyc; MetaCyc:MONOMER-17577; -.
DR   SABIO-RK; Q9UUZ3; -.
DR   UniPathway; UPA00280; -.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
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; IPR041625; Beta-mannosidase_Ig.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..931
FT                   /note="Beta-mannosidase A"
FT                   /id="PRO_0000012168"
FT   ACT_SITE        479
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
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        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        608
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        738
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        790
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        798
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        830
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        918
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   931 AA;  104390 MW;  D296E185EA3BF430 CRC64;
     MRHSIGLAAA LLAPTLPVAL GQHIRDLSSE KWTLSSRALN RTVPAQFPSQ VHLDLLRAGV
     IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYGSTWLV FDGLDTFATI SILWTANRIH
     GQSVSPVSGS MYLPALEACQ RRILIRKVSF RGGVTAEVNT CYLHIEWPDD VQLTYEYPNR
     WFMRKEQSDF GWDWGPAFAP AGPWKPAYIV QLDKKESVYV LNTDLDIYRK NQINYLPPDQ
     SQPWVVNASI DILGPLPAKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLN
     PKLWWPQSSV IRTSTMFLSL SKVEGTRPWP VWTNGRASAP FFLNQRNITE VQRAQGIAPG
     ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EERISRLFDA VVVGNQNMLR VWSSGAYLHD
     YIYDLADEKG ILLWSEFEFS DALYPSDDAF LENVAAEIVY NVRRVNHHPS LALWAGGNEI
     ESLMLPRVKD AAPSSYSYYV GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA
     PVPMAERYDN TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV
     DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVISYYPIP SKSDHISNFS
     AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE DIWQAPSWAG IEYGGRWKVL
     HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK
     SVPFTVGGLN STRIYGTNVS SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS
     WPKDLKIVDP GLKLGYSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK
     EIGFTVLDDT TNGAWVRNIT VQSLWDQKVR G
//