位置:首页 > 蛋白库 > MANBA_ASPNC
MANBA_ASPNC
ID   MANBA_ASPNC             Reviewed;         931 AA.
AC   A2QWU9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=An11g06540;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270241; CAK96951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QWU9; -.
DR   SMR; A2QWU9; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PaxDb; A2QWU9; -.
DR   PRIDE; A2QWU9; -.
DR   EnsemblFungi; CAK96951; CAK96951; An11g06540.
DR   HOGENOM; CLU_005015_3_0_1; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000006706; Chromosome 7R.
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; 2.60.40.10; -; 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   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF17753; Ig_mannosidase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 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..931
FT                   /note="Beta-mannosidase A"
FT                   /id="PRO_5000220610"
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        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
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;  104026 MW;  C3D32E4763723612 CRC64;
     MRHSIGLAAA LLAPTLPVAL GQYIRDLSTE KWTLSSRALN RTVPAQFPSQ VHLDLLRAGV
     IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYDSTWLV FDGLDTFATI SFCGQQIAST
     DNQFRQYAFD VSTALGSCKG DPVLSINFGS APNIVDAIAQ DSNSQKWPDD VQLTYEYPNR
     WFMRKEQSDF GWDWGPAFAP AGPWKPAYIV QLDKKESVYV LNTDLDIYRK GQINYLPPDQ
     SQPWVVNASI DILGPLPTKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLT
     PKLWWPQGLG DQNLYNVSIT VQSRGNQTVA SVNKRTGFRT IFLNQRNITE AQRAQGIAPG
     ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EEKMSRLFDA VVVGNQNMLR VWSSGAYLHD
     YIYDLADEKG ILLWSEFEFS DALYPSDDAF LENVAAEIVY NVRRVNHHPS LALWAGGNEI
     ESLMLPRVKD AAPSSYSYYV GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA
     PVPMAERYDN TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV
     DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVVSYYPIP SKSDHISNFS
     AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE DIWQAPSWAG IEYGGRWKVL
     HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK
     SVPFTVGGLN STRIYGTNVS SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS
     WPKDLKIVDP GLKIGHSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK
     EISFTVLEDT TDGAWVRNIT VQSLWDQKVR G
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024