MANBA_ASPTN
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 03-AUG-2022, entry version 74.
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;
OC Aspergillus subgen. 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};
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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 PRIDE; Q0CI48; -.
DR GeneID; 4321960; -.
DR eggNOG; KOG2230; Eukaryota.
DR OrthoDB; 517710at2759; -.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
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; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF49303; SSF49303; 1.
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; 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
