MANBA_ASPFN
ID MANBA_ASPFN Reviewed; 914 AA.
AC B8NP78;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=AFLA_128610;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963481; EED48638.1; -; Genomic_DNA.
DR RefSeq; XP_002382054.1; XM_002382013.1.
DR AlphaFoldDB; B8NP78; -.
DR SMR; B8NP78; -.
DR STRING; 5059.CADAFLAP00009919; -.
DR PRIDE; B8NP78; -.
DR EnsemblFungi; EED48638; EED48638; AFLA_128610.
DR VEuPathDB; FungiDB:AFLA_128610; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_3_0_1; -.
DR OMA; PFWNYTT; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000001875; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..914
FT /note="Beta-mannosidase A"
FT /id="PRO_0000394645"
FT ACT_SITE 462
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 744
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 784
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 914 AA; 102929 MW; F6DAC075C591E64B CRC64;
MRFTATAAAL VASSIPATLG QHVRDLSNEK WTLSSDALNH TVPGNLPSHA HLDLLKAGVI
DDPYHGLNDF NLRWIPESNW TYTTDKIKDL MPIEFCGKYV ASTNNQYRQY SFDVSQILEG
CNEDPILKID FGSAPNIVNA IAEDRNSPVW PDGIQQTYEY PNRWFMRKEQ SDFGWDWGPA
FAPAGPWKPA YIVQLPKAQN IHVLNTDLDI YRKGQINHLP PDQSQPWVVN ASIDFVGSLP
PNPSMSIEFK DTKSGEILTS KRIGNVTVSG NSVTGVTVLG GVTPKLWWPL GLGDQNLYNI
TVTVTGHQNQ TLAHVTKRTG FRTIFLNQRN ITDAQLAQGI APGANWHFEV NGHEFYAKGS
NIIPPDAFWP RVTEARMARL FDAVVAGNQN MLRVWSSGIY LHDFIYDLAD ERGILLWSEF
EFSDALYPVD DAFLDNIAAE VVYNVRRVNH HPSLALWAGG NEIESLMLPT VERKAPEEYA
KYVGEYEKLY ISLILPLVYQ NTRSITYSPS STTEGYLDVD LSAPVPMVER YHNTTPGSYY
GDTDFYNYDS SVSFNSHVYP VGRFANEFGY HSMPSLQTWQ QAVDPEDLHF NSTTVMLRNH
HYPAGGTFTD NFHNTSLGMG EMTIAVQRYY PIPNKLDSVA NFSAWCHATQ LFQADMYKSE
IQFYRRGSGM PERQLGSLYW QLEDIWQAPS WAGIEYGGRW KVLHYVSRDI YQRIIVSPFW
NYTTGDLDLY VTSDLWESAK GKVNLTWLDL SGTPLPHNAG TPGSVPFNVG ALNTTKIYST
NIKNLTLPNP KDAILVLSLS GEGHLPNSDK KTTFTHQNHF TPVFPKDLAL VDPGLELSYN
TKSKTFTVEA KSGVSLYTWL DYPADVVGYF DENAFVLLPG QKKEIGFTVQ EDNTDGKWVQ
GVTVQSLWNQ TLEK
