MANBA_ASPNG
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 03-AUG-2022, entry version 84.
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 VEuPathDB; FungiDB:An11g06540; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1160135; -.
DR VEuPathDB; FungiDB:ATCC64974_92080; -.
DR VEuPathDB; FungiDB:M747DRAFT_299830; -.
DR BioCyc; MetaCyc:MON-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; 2.60.40.10; -; 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 Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 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
