MANBA_ASPFC
ID MANBA_ASPFC Reviewed; 926 AA.
AC B0Y7S2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=AFUB_074800;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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}.
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DR EMBL; DS499599; EDP49453.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y7S2; -.
DR SMR; B0Y7S2; -.
DR EnsemblFungi; EDP49453; EDP49453; AFUB_074800.
DR VEuPathDB; FungiDB:AFUB_074800; -.
DR HOGENOM; CLU_005015_3_0_1; -.
DR PhylomeDB; B0Y7S2; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000001699; 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; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..926
FT /note="Beta-mannosidase A"
FT /id="PRO_0000394644"
FT ACT_SITE 474
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 905
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 926 AA; 103736 MW; 0926E59CD2AE6E7A CRC64;
MHVKAETVLA LLTPAPPSVV GQHVVDLSGD GWTLSSTALN RTVPGHLPSQ VHLDLFEAGV
IDIMASMILT FVGLRMPIGR IPATRLKAYF ESTWLVFDGL DTFATITFCD QHVGSTDNQF
RQHHFDVSQI LKECKQDPVL RINFGSAPNI ANTIAKSPDA EEWPPGVQIT NEYPNRWYIR
KEQSDFGWDW GPAFAPVGPW KPSYIVQNSH AELYVLNTDI DIYRQGQINY LPPDQSQPWI
VNASIDFLGP VPCKPSMSIE IKDAATGSVL SSGLLQNVTV SGKSITGTTT IDGDAPKLWW
PSGMGKQNLY NVTITVQNDM KKSLAKVTKR TGFRTIFLNQ RNITDDQLAQ GIAPGANWHF
EINGYEFYAK GSNIIPPDAF WPRVTQARMA RLFDAVTAGN QNMLRVWASG AYLHDFIYDL
ADEKGILLWS EFQFSDALYP VNDAFLENVA AEVVYNVRRV NHHPSLALWA GGNEIESLML
PMARRADPTG YSKYIGEYEK LYISLILPLV YENTRSITYS PSSTTEGYLY VNLSAPVPMA
ERYSNTTPGS YYGDTDYYNY DTSVSFDYNH YPVGRFANEF GFHSMPSLQT WQQAVDPEDL
QFNSSVVVLR NHHYTAGGLF TDNFKNSSKG MGEMTMGVEA YYPIPSKSDS VANFSAWCHA
TQLFQADLYK SQIQFYRRGS GMPERQLGSL YWQLEDIWQA PTWAGIEYDG RWKVLHYVAR
DIYQPIIVSP FWNYTTGRLE VYVTSDLWEP AQGTVNLTWV DLSGKSIANN AGTPETVSFT
VGALNTTNIY TTNISELSLP DLKDSILILS LSGEGRLPNA SSKKAFVHQN HFTPVFPKDL
SLKDPKLEVS YSPESRKFTV QATGGVSLYT WLDYPAGAVG YFEANAFVLL PGVPKEVSFV
AQEGNVTDDW LQRVTVQSLW DQKVRD
