ID MANBA_ASPTN Reviewed; 932 AA. AC Q0CI48; DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot. DT 19-MAR-2014, sequence version 2. DT 02-SEP-2026, entry version 85. 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=ATEG_06636; OS Aspergillus terreus (strain NIH 2624 / FGSC A1156). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati. OX NCBI_TaxID=341663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH 2624 / FGSC A1156; RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K., RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., RA Nierman W.C., Milne T., Madden K.; RT "Annotation of the Aspergillus terreus NIH2624 genome."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 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. 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 -!- SEQUENCE CAUTION: CC Sequence=EAU33180.1; Type=Erroneous gene model prediction; Evidence={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; CH476602; EAU33180.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_001215814.1; XM_001215814.1. DR AlphaFoldDB; Q0CI48; -. DR SMR; Q0CI48; -. DR STRING; 341663.Q0CI48; -. DR GlyCosmos; Q0CI48; 17 sites, No reported glycans. DR EnsemblFungi; EAU33180; EAU33180; ATEG_06636. DR GeneID; 4321960; -. DR eggNOG; KOG2230; Eukaryota. DR OrthoDB; 2866996at2759; -. DR UniPathway; UPA00280; -. DR Proteomes; UP000007963; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006516; P:glycoprotein catabolic process; IEA:TreeGrafter. DR FunFam; 2.60.120.260:FF:000200; Beta-mannosidase A; 1. DR FunFam; 2.60.40.10:FF:001511; Beta-mannosidase A; 1. DR FunFam; 2.60.40.10:FF:002310; Beta-mannosidase A; 1. DR FunFam; 3.20.20.80:FF:000084; Beta-mannosidase A; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR InterPro; IPR036156; Beta-gal/glucu_dom_sf. DR InterPro; IPR054593; Beta-mannosidase-like_N2. DR InterPro; IPR050887; Beta-mannosidase_GH2. DR InterPro; IPR041625; Beta-mannosidase_Ig. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR006102; Ig-like_GH2. DR InterPro; IPR041447; Mannosidase_ig. DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1. DR PANTHER; PTHR43730:SF5; BETA-MANNOSIDASE A; 1. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF22666; Glyco_hydro_2_N2; 1. DR Pfam; PF17753; Ig_mannosidase; 1. DR Pfam; PF17786; Mannosidase_ig; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; KW Polysaccharide degradation; Reference proteome; Secreted; Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..932 FT /note="Beta-mannosidase A" FT /id="PRO_0000394648" FT ACT_SITE 480 FT /note="Proton donor" FT /evidence="ECO:0000250" FT CARBOHYD 41 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 81 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 261 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 284 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 289 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 318 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 348 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 538 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 551 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 609 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 624 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 632 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 659 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 739 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 791 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 932 AA; 105189 MW; 2B1436F3E4E53D88 CRC64; MRVPAQATIA VLASAVSSPL NDPQIYDLGK LGWTLSSPAL NRTVPGHLPS QVHLDLLRAG VIDDPYHDLN DFNLRWIADA NWTYTSDPIR GLGNNTHSTW LVFEGLDTFA TIKYCDKQIA STNNQFRQYA FDISEAVKDC TADPVLSLNF GSAPKIVDQI AADPASPQWP FGIQQSYEYP NRWFMRKEQS DFGWDWGPAF APAGPWKPAY LVQLSSEQNV HVLNTDLDIY RQGQINYLPP DQTQPWVLNA SIDFFGSLPS NSSMSIAISE TNSGAELTTQ SLRNITILNG SITGVAVLKD ASPKLWWPYG LGEQNLYNVT ITVSDGVRSL ARVTKRTGFR TIFLNQRNIT DTEIAQGVAP GAHWNFEVNG HEFYAKGSNL IPPDAFWARV TTTKMARLFD SVVAANQNML RVWSSGAYLP DFMYDLADER GVLLWSEFEF SDAMYPVDKA FLDNVAAEVV YNVRRVNHHP SLALWAGGNE IESLILPTIE RSYPDQYAKY VGDYETLYIN LILPLVYENT HSITYSPSST TEGYLDVNLS AKIVMAERYQ NLTEGHYYGD TDYYNYDTSV AFDFSQYPVG RFANEFGFHS MPSLQSWQQA VDPEDLHFNS SVIMLRNHHY PAGNLSTHNF HNTSMGMGET TMGVMNYYPV PDKTDPIANF SAWCHATQLF QADFYKSQIQ FYRRGSGMPE RQLGSLYWQL EDIWQAPSWA GIEYDGRWKV LHYVARDIYQ PVIVSPFWNS TTRRLDVYVT SDLWEPVSGT VDLAWMDLSG KPIAQNARTP KTAAFVVGAL NTTKIYSMNI NERALPDPKN SVLILSVQAE GHLPNSNKKS TLTHQGHFTP VFPKDLMLVD PHLELRYNAK TLTFTVQAKA GVSLYTWLDY PAGVVGYFED NGFVLVPGQK RDIRFVMQED KTDGNWVQDV TVRSLWDQTT KT //