MANBA_ASPCL
ID MANBA_ASPCL Reviewed; 932 AA.
AC A1CTM5;
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 A;
DE EC=3.2.1.25;
DE AltName: Full=Mannanase A;
DE Short=Mannase A;
DE Flags: Precursor;
GN Name=mndA; ORFNames=ACLA_083570;
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. 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 ---------------------------------------------------------------------------
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; DS027060; EAW06662.1; -; Genomic_DNA.
DR RefSeq; XP_001268088.1; XM_001268087.1.
DR AlphaFoldDB; A1CTM5; -.
DR SMR; A1CTM5; -.
DR STRING; 5057.CADACLAP00007511; -.
DR EnsemblFungi; EAW06662; EAW06662; ACLA_083570.
DR GeneID; 4700372; -.
DR KEGG; act:ACLA_083570; -.
DR VEuPathDB; FungiDB:ACLA_083570; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_3_0_1; -.
DR OMA; PFWNYTT; -.
DR OrthoDB; 517710at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000006701; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..932
FT /note="Beta-mannosidase A"
FT /id="PRO_0000394643"
FT ACT_SITE 480
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
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 609
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 762
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; 104680 MW; AFDBB74995D092FD CRC64;
MRIREQTILA LLSPGLPPVT GQHVLDLSEP GWTVSSKALN RTVPGRLPSQ VHLDLFEAGV
IATMGSMILT FAGLRMPTGR TPATLLLGCE LTDHESTWLV FDGLDTFTTI TFCDQIIGST
YNQFRQYHFD VSQVLKECKQ EGPVLSINFG SAPNIANAIA NGPSAEEWPA GVQITNEYPN
RWYIRKEQSD FGWDWGPAFA PAGPWKPAYI VQNKNPDRLY VLNTDLDIYR RGQINHLPPD
QSQSWVVNAS IDVLGSVPQW PSMSVEIKDA YSGVVLSSGL LENVTVSGNS VTGVTVVDGR
TPKLWWPNGM GDQSLYNVTI AVHNHRNQVV AEVMKRTGFR TIFLNQRNIT EEQLAQGVAP
GANWHFEING REFYAKGSNI IPPDAFWPRV TPSRMERLFD AVTAGNQNML RVWASGAYLH
DFIYDLADEK GILLWSEFQF SDALYPVDDA FLENVAAEVV YNVRRVNHHP SLALWAGGNE
IESLMLPMVR RADHKGYAKY VGEYEKLYIS LILPLVYENT RSITYSPSST TEGYLHVNLS
APVPMTERYS NTTPGSYYGD TDYYNYDTSV SFNYHKYPVG RFANEFGFHS MPSLQTWQQA
VDPKDLYFNS SVVVLRNHHY TAGGLFTDNY QNSSRGMGEM TMGVESYYPI PSKSDPVANF
SAWCHATQLF QADMYKAQIQ FYRRGSGMPE RQLGSLYWQL EDTWQAPTWA GIEYDGRWKM
LHYVARDIYE PIIVSPFWNY TTGDLEVYVT SDLWEPAQGT VNLTWVDLSG KSIAGNAGTP
ESIPFSVGAL NATDVYSANV ADLSPPDLTD SILILSLAGE GYLPNARTRS EFRHENQFTP
VFPKDLALRD PKLELAYNPD TRTFTVEATA GVSLYTWLDY PAGVVGYFEQ NGFVLLPGMK
KEIGFVVQEG SVDEDWMRSV TVTSLWDQKV RE
