MANBB_EMENI
ID MANBB_EMENI Reviewed; 843 AA.
AC Q5B7W2; C8VHQ6; Q1HFT6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
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=AN3368;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
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. Releases the
CC terminal mannose residue from mannobiose, mannotriose and galactosyl-
CC mannotriose (GM3), but not from galactosyl-mannobiose (GM2) or di-
CC galactosyl-mannopentaose (G2M5). {ECO:0000269|PubMed:16844780,
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.22 mM for p-nitrophenyl-beta-mannopyranoside
CC {ECO:0000269|PubMed:24021641};
CC Note=kcat is 79.2 min(-1) with p-nitrophenyl-beta-mannopyranoside as
CC substrate.;
CC pH dependence:
CC Optimum pH is 6. Active from pH 5 to 8.
CC {ECO:0000269|PubMed:24021641};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius (at pH 6).
CC {ECO:0000269|PubMed:24021641};
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:0000305|PubMed:24021641}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC mannosidase B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF82847.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA63336.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ490488; ABF50864.1; -; mRNA.
DR EMBL; AACD01000055; EAA63336.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF82847.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_660972.1; XM_655880.1.
DR AlphaFoldDB; Q5B7W2; -.
DR SMR; Q5B7W2; -.
DR STRING; 162425.CADANIAP00009674; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblFungi; EAA63336; EAA63336; AN3368.2.
DR GeneID; 2874350; -.
DR KEGG; ani:AN3368.2; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_1_0_1; -.
DR InParanoid; Q5B7W2; -.
DR OrthoDB; 517710at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004567; F:beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR GO; GO:0046355; P:mannan catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..843
FT /note="Beta-mannosidase B"
FT /id="PRO_0000394658"
FT ACT_SITE 432
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 843 AA; 96367 MW; 53B99E1C93DB4055 CRC64;
MGAFTQHVLS EGWSFKDSGD QSPDAWLSVP TVPSVVHQDL QANGKLDDPF IGLNELSARW
VNEKSWTYRN VFQKPTVPAG SSIFLVFDGL DTFAKVKLDG QVILESDNMF LAHRVDITKA
LDVEGEHTLE IDFDCALLRA RELRKQHPDH KWVGFNGDTA RLSVRKAQYH WGWDWGPVLM
TAGIWKEVRL EVYSAKISDL WTEVHLAEDH SKARITAAAE VETQGTGNSY KATFTLSLQG
QQIGKEVATL DGNVAKTTFD VQEPSLWWPN GYGDQTLYEI SVSLEKEEEQ AHQVSKKFGI
RTAEVIQRPD KHGKSFFFRI NGVDIFCGGA CWIPADSLLT NITPDRYRKW IELMAVGHQV
MIRVWGGGIY EDESFYQACD EVGVMVWQDF MFGCGNYPTW PEILESIEKE AEYNLRRLRH
HPSIVIWVGN NEDYQVQEQQ GLTYNYADKD PESWLKTDFP ARYIYEHLLP KAVQKIIPSA
YYHPGSPWGD GKITSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
DHFVTNEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLEVYIYL TQVVQAETMM
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVS RVLKPLAIGV
RREHHDWSVS HAQPPKTSKY ELWVVSSLLK EVIGKVELRF ISIKTGLAIH ESIVRENVTI
VPNGTTNILD GVIDHAVDEP HVLAARLWVD GELVARDVDW PQPFKYLDLS DRGLEITRIS
KTESEQVLEL SARKPVKCLV FEERDNVRVS DSAIDIVPGD EQFVTIKGLK RSDAPLKYKF
LGQ
