MANBB_ASPCL
ID MANBB_ASPCL Reviewed; 845 AA.
AC A1CGA8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=ACLA_066240;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027053; EAW10988.1; -; Genomic_DNA.
DR RefSeq; XP_001272414.1; XM_001272413.1.
DR AlphaFoldDB; A1CGA8; -.
DR SMR; A1CGA8; -.
DR STRING; 5057.CADACLAP00006175; -.
DR EnsemblFungi; EAW10988; EAW10988; ACLA_066240.
DR GeneID; 4704556; -.
DR KEGG; act:ACLA_066240; -.
DR VEuPathDB; FungiDB:ACLA_066240; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_1_0_1; -.
DR OMA; MFANFDY; -.
DR OrthoDB; 517710at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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; -; 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_0000394651"
FT ACT_SITE 432
FT /note="Proton donor"
FT /evidence="ECO:0000250"
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; 96760 MW; 41EE1CB40C7719C7 CRC64;
MAALQRFPLS KGWSFKDSED KSEDAWMPVP VVPSVVQQDL QANNKLKDPY IGFNELETRW
VNEKSWTYKT TFQKPAVPAG SAIFLAFDGL DTFATVKLDG NVILESDNMF LAHRLDVTKA
LEAEGDHSLE IDFDCAFLRA KELRKQDSKH NWASFNGDPS RLSVRKSQYH WGWDWGPVLM
TAGIWREVRL EVYTARVADL WTDVQLASDH QNAQITAFAE VESVNSDAHK ARFTLSLHGQ
ELGREEVSVS EDGSAKVSFD VKSPSLWWPH GYGDATLYEV SVSLVKDQDE VHQVSKKFGI
RTAEVVQQPD KHGKSFFFRV NGVDIFCGGS CWIPADNYLP SVTADRYRKW IELMVHGRQV
MIRVWGGGNY EDDSFYDACD ELGVLVWQDF MFGCGNYPTW PNLLESIRKE SVYNVRRLRH
HPSIVVWVGN NEDYQVQESA GLTYDFEDKN PENWLKTDFP ARYIYEKILP EVVEEYSPST
FYHPGSPWGD GKTTSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
DYFVENEADK FPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETHVYL TQVVQAETMM
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLNPIAVGV
RREHHDWSVT HAQPPKTSKF ELWVASSLQK EVQGTVELRF LSINTGLEVR ERIVHENVSI
VPNGTTNLIV DGLIDYKVHP EPHVLAVRIW VNGELVARDV DWPQPFKYLD LSNRGLEVKL
VSESENEQTL LLSAQKPVKC LVFEEREGVR ISDSAIDIVP GDEQRVTIKG MKPGDAPLKY
KFLGQ