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MANBB_ASPFU
ID   MANBB_ASPFU             Reviewed;         845 AA.
AC   Q4WAH4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Beta-mannosidase B;
DE            EC=3.2.1.25;
DE   AltName: Full=Mannanase B;
DE            Short=Mannase B;
GN   Name=mndB; ORFNames=AFUA_7G01320;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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. Prefers mannobiose over mannotriose
CC       and has no activity against polymeric mannan. Is also severely
CC       restricted by galactosyl substitutions at the +1 subsite (By
CC       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   -!- MISCELLANEOUS: In contrast to clade A beta-mannosidases, which are
CC       likely secreted, clade B proteins appear to be intracellular.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC       mannosidase B subfamily. {ECO:0000305}.
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DR   EMBL; AAHF01000015; EAL84762.1; -; Genomic_DNA.
DR   RefSeq; XP_746800.1; XM_741707.1.
DR   AlphaFoldDB; Q4WAH4; -.
DR   SMR; Q4WAH4; -.
DR   STRING; 746128.CADAFUBP00008544; -.
DR   EnsemblFungi; EAL84762; EAL84762; AFUA_7G01320.
DR   GeneID; 3504183; -.
DR   KEGG; afm:AFUA_7G01320; -.
DR   VEuPathDB; FungiDB:Afu7g01320; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_1_0_1; -.
DR   InParanoid; Q4WAH4; -.
DR   OMA; MFANFDY; -.
DR   OrthoDB; 517710at2759; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0004567; F:beta-mannosidase activity; IBA:GO_Central.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
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; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
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.
FT   CHAIN           1..845
FT                   /note="Beta-mannosidase B"
FT                   /id="PRO_0000394654"
FT   ACT_SITE        432
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        717
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        723
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   845 AA;  96998 MW;  B6EA86796A8C33DE CRC64;
     MSKLQQFPLS KGWSFRDNEA TSEDAWMPVP VVPSVVHQDL QANNKLKDPY IGFNELEARW
     VNEKSWTYKT VFQKPAAPAG SCIVLAFDGL DTFAKVKLDG NVILENDNMF LARRVDVTKA
     LEAEGDHVLE IDFDCAFLRA KELRKQDPRH NWASFNGDPS RLSVRKAQYH WGWDWGPVLM
     TAGIWREVRL EVYSARVADL WTEVQLASDH QSAQVTAFVE VESVHSGSHR ACFTLSLHGQ
     EITREEIGVT ENGTAKATFD VKEPSLWWPH GYGDATLYEV SVSLVKEQEE LHRVSKKFGI
     RTAEVIQRPD KHGKSFFFRV NGVDIFCGGS CWIPADNLLP SITAERYRKW IELMVHGRQV
     MIRVWGGGIY EDNSFYDACD ELGVLVWQDF MFGCGNYPTW PNLLESIRKE SVYNVRRLRH
     HPSIVIWVGN NEDYQVQEQA GLTYNYEDKD PENWLKTDFP ARYIYEKLLP EVVQEYSPGT
     FYHPGSPWGD GKTTSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
     DYFVENEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETHIYL TQVVQAETMM
     FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLNPIAVGV
     RREHHDWSVT HAQPPKTSKF ELWVASSRQQ EIQGTVELRF LSVNTGLEVR ERIVHENVSI
     VPNGTTNLIV DGLIDHTVHS EPHVLAARIW VDGQLVARDV DWPQPFKYLD LSDRGLEVKK
     ISESEDEQTL LISTKKPVKC LVFEEREGVR ISDSAMDIVP GDDQRVTIKG LKPGDAPLKY
     KFLGQ
 
 
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