MANBA_ASPAC
ID MANBA_ASPAC Reviewed; 937 AA.
AC O74168;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 89.
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; Synonyms=manB;
OS Aspergillus aculeatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 55-71; 186-189;
RP 265-274; 411-424 AND 805-819, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=F-50;
RX PubMed=10052144; DOI=10.1271/bbb.63.206;
RA Takada G., Kawaguchi T., Kaga T., Sumitani J., Arai M.;
RT "Cloning and sequencing of beta-mannosidase gene from Aspergillus aculeatus
RT no. F-50.";
RL Biosci. Biotechnol. Biochem. 63:206-209(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=F-50;
RA Arai M., Fujimoto H., Ooi T., Ogura S., Murao S.;
RT "Purification and properties of a beta-mannosidase from Aspergillus
RT aculeatus.";
RL J. Appl. Glycosci. 42:49-51(1995).
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. Releases the terminal mannose
CC residue from mannotriose and is somewaht less active on other
CC mannooligosaccharides. {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues
CC in beta-D-mannosides.; EC=3.2.1.25; Evidence={ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 2.0. Stable from pH 4 to pH 7. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10052144,
CC ECO:0000269|Ref.2}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10052144}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC mannosidase A subfamily. {ECO:0000305}.
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DR EMBL; AB015509; BAA29029.1; -; Genomic_DNA.
DR AlphaFoldDB; O74168; -.
DR SMR; O74168; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR CLAE; MND2B_ASPAC; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_39980; -.
DR UniPathway; UPA00280; -.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..937
FT /note="Beta-mannosidase A"
FT /id="PRO_0000394642"
FT ACT_SITE 482
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 937 AA; 104216 MW; 0F6200BEB03D704B CRC64;
MRALPTTATT LLGVLFFPSA SRSQYVRDLG TEQWTLSSAT LNRTVPAQFP SQVHMDLLRE
GIIDEPYNDL NDFNLRWIAD ANWTYTSGKI EGLGEDYEST WLVFDGLDTF ASISFCGQFV
GATDNQFRQY MFDVSSILKA CPEEPTLGIQ FGSAPNIVDA IAQDPSSPTW PEGVQITYEY
PNRWFMRKEQ SDFGWDWGPA FAPAGPWKPG YVVQLKQAAP VYVRNTDLDI YRLGQINYLP
PDQTQPWVVN ASLDYLGSLP ENPSMAIEVK DLQSGEILAS RPLTNITVTE GSVTGVTVLE
GVDPKLWWPQ GLGDQNLYNV TISVTDGGNQ SVAEVTKRTG FRTIFLNQRN ITDAQLAQGI
APGANWHFEV NGHEFYAKGS NLIPPDCFWT RVTEDTMTRL FDAVVAGNQN MLRVWSSGAY
LHDYIYDLAD EKGILLCSEF QFSDALYPTD DAFLENVAAE VVYNVRRVNH HPSLALWAGG
NEIESLMLLL VEAADPESYP FYVGEYEKMY ISLFLPLVYE NTRSISYSPS STTEGYLDID
LSAPVPMAER YSNTTEGEYY GDTDHYNYDA SIAFDYGTYP VGRFANEFGF HSMPSLQTWQ
QALTDPADLT FNSSVVMLRN HHYPAGGLMT DNYHNTVARH GRNDPGRAGL LPDAQHSVRP
RGQLQRLVPR DPALPGGPLQ VTNPVLPAGQ RAARTPARVP VLAARGHLAG ALVGGDRVRR
PLEGPHYVAR DIYKPVIVSP FWNYTTGALD IYVTSDLWTA AAGSVTLTWR DLSGKPIASN
GGLPTKPLPF HVGALNSTRL YRMNMKQQPL PRHEDAILAL ELTATGSLPN TDEEVTFTHE
QWFTPAFPKD LDLVNLRVRV EYDAPLGKFA VEATAGVALY TWLEHPEGVV GYFEENSFVV
VPGQKKVVGF VVQADETDGE WVHDVTVRSL WDLNEGE
