MANBA_NEOFI
ID MANBA_NEOFI Reviewed; 930 AA.
AC A1DMT2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=NFIA_054490;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027698; EAW16103.1; -; Genomic_DNA.
DR RefSeq; XP_001258000.1; XM_001257999.1.
DR AlphaFoldDB; A1DMT2; -.
DR SMR; A1DMT2; -.
DR STRING; 36630.CADNFIAP00004919; -.
DR EnsemblFungi; EAW16103; EAW16103; NFIA_054490.
DR GeneID; 4584515; -.
DR KEGG; nfi:NFIA_054490; -.
DR VEuPathDB; FungiDB:NFIA_054490; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_3_0_1; -.
DR OMA; PFWNYTT; -.
DR OrthoDB; 517710at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000006702; 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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..930
FT /note="Beta-mannosidase A"
FT /id="PRO_0000394650"
FT ACT_SITE 478
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 737
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 930 AA; 104276 MW; 736EDACC02D252D3 CRC64;
MHVKAETVLA LLTPGLPSVV GQHVVDLSGD GWTLSSTALD RTVPGHLPSQ VHLDLFEAGV
INITASMILT FVGLLMPIGR IPATRLKACD LENFESTWLV FDGLDTFTTI TFCDQHVGST
DNQFRQYHFD VSQILKECKQ DPVIRINFGS APSIANAIAK SPDAEEWPPG VQITNEYPNR
WYIRKEQSDF GWDWGPAFAP VGPWKPSYIV QNNHAELYVL NTDLDFYRQG QINYLPPDQS
QPWIVNASID ILGPVPWKPS MSIEIKDAAT GSVLSSGLLQ NVTVSGNSIT GTTTIDGDAP
KLWWPSGMGE QNLYNVTVTV QNDKKKSLAK VTKRTGFRTI FLNQRNITDD QLAQGIAPGA
NWHFEINGHA FYAKGSNIIP PDAFWPRVTQ ARMARLFDAV TAGNQNMLRV WASGAYLHDF
IYDLADEKGI LLWSEFQFSD ALYPVNDAFL ENVAAEVVYN VRRVNHHPSL ALWAGGNEIE
SLMLPMVKRA DPTGYSKYVG EYEKLYISLI LPLVYENTRS ITYSPSSTTE GYLYVNLSAP
VPMAERYSNT TPGSYYGDTD YYNYDTSVSF DYNHYPVGRF ANEFGFHSMP SLQTWQQAVD
PEDLHFNSSV VMLRNHHYTA GGLFTDNFKN SSKGMGEMTM GVEAYYPIPS KSDSVANFSA
WCHATQLFQA DMYKSQIQFY RRGSGMPERQ LGSLYWQLED IWQAPTWAGI EYDGRWKVLH
YVARDIYQPI IVSPFWNYTT GRLEVYVTSD LWEPAQGTVN LTWVDLSGKT IANNAGTPET
VNFTVGALNT TNIYTTNISE LSLPDLKDSI LILSLSGEGR LPNTSSKKAF VHQNHFTPVF
PKDLSLKDPK LEISYSPESR KFTVQATGGV SLYTWLDYPA GAVGYFEENA FVLLPGVQKE
VSFAAQEGNV TDDWVRRVTV QSLWDQKVRD
