MANBB_ASPOR
ID MANBB_ASPOR Reviewed; 844 AA.
AC Q2TXB7;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 3.
DT 25-MAY-2022, entry version 85.
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=AO090010000208;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP GENE MODEL REVISION.
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. 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE66106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007175; BAE66106.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001827239.2; XM_001827187.2.
DR AlphaFoldDB; Q2TXB7; -.
DR SMR; Q2TXB7; -.
DR STRING; 510516.Q2TXB7; -.
DR ChEMBL; CHEMBL4155; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR VEuPathDB; FungiDB:AO090010000208; -.
DR UniPathway; UPA00280; -.
DR PRO; PR:Q2TXB7; -.
DR Proteomes; UP000006564; Chromosome 8.
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; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..844
FT /note="Beta-mannosidase B"
FT /id="PRO_0000394656"
FT ACT_SITE 432
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 844 AA; 95960 MW; 4FBC82ACDB12075A CRC64;
MAAFSQYPLS TGWSFKDSDD QSPEAWMPVP VVPSVAHQDL QANQKLKNPY IGFNELDARW
VNDKSWTYRT VFQKPAVAAG SSIILAFDGL DTFATVKLDG SVILQSDNMF LAHRVDVTKA
LEAEGDHVLE IDFDCAMRRA RELREKDTKH NWASFNGDPA RMAVRKAQYH WGWDWGPLLS
TAGIWREVRL EVYSAKISDL WTEVELASDH QTARVSAFAE VDAADSVDSY KASFLLSLHG
KEVAREVATL KDKVANVTFD VTQPSLWWPN GYGDPALYEI SVSLEKEDCE IHSVSKKIGI
RTAELIQQPD RHGKSFFFRI NGVDVFCGGS CWIPADNLLP SITAERYRKW IELMVAGRQV
MIRVWGGGCY EDDSFYQACD ELGVLVWQDF MFGCGNYPTW PELLESIEKE ANYNVRRLRH
HPSIVVYVGN NEDYQVQESA GLVYDYEDKN PENWLKTDFP ARYIYEKLLP SVVEKLSPKT
VYHPGSPWGD GKITSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
EYFVENEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYVYL TQVVQAETMM
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLKPIAVGV
RREHHDWSVT HAQPPKTSKY ELWIASSLQK ETVGTIELRF LSVNTGLDVR APILRDNVKI
VPNGTTNILE GVIDHKAQPE PHVLAARLWV DGEVTARDVD WPQPFKYLDL SDRGLEVNKV
SESGNEQKLL ITAKKPVKCL VFEERDGIRV SDSAMDIVPG DGQTVTVTGL KAGDAPLKYK
YLGQ