ID A0A1L9P9H8_ASPVE Unreviewed; 925 AA.
AC A0A1L9P9H8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Beta-mannosidase A {ECO:0000256|ARBA:ARBA00021795};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Mannanase A {ECO:0000256|ARBA:ARBA00031061};
GN ORFNames=ASPVEDRAFT_37634 {ECO:0000313|EMBL:OJI98189.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJI98189.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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 Evidence={ECO:0000256|ARBA:ARBA00000829};
CC -!- PATHWAY: Glycan metabolism; N-glycan degradation.
CC {ECO:0000256|ARBA:ARBA00004740}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC mannosidase A subfamily. {ECO:0000256|ARBA:ARBA00007483}.
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DR EMBL; KV878126; OJI98189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9P9H8; -.
DR STRING; 1036611.A0A1L9P9H8; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_37634; -.
DR OrthoDB; 2504097at2759; -.
DR UniPathway; UPA00280; -.
DR Proteomes; UP000184073; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF5; BETA-MANNOSIDASE A; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000184073};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 242..335
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 736..838
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 841..920
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 925 AA; 104163 MW; F2231CD32B2F0D0E CRC64;
MKFLEFGTQA VIASSVAWDR HIMDLGTVNW SLSGPALNTT VPASIPSHVH LDLFNAGVID
DPYYGLNEIS LRWIGESNWT YTSDPISDLL REYESTWLVF DGLDTFATIS FCGHHIASTN
NQFRQYAFDV SSPLKECNGD PIISIDFASA PKTVDAIAAD PSSPQWPVQL TSQYPNRWFM
RKQQCDFGWD WGPAFAPAGP WKPAYLVQLE KPGNIHVLNT DLDIYRQGSI NHLPPDQNKP
WVVNASIDFI GNPPAEPQLS IEIKDIESGE VLASQTAEAV NVTETSITGV TTFDDLSPKL
WWPSGLGAQS LYNVTITVHD GSEQTALVSK RTGFRTIFLN QRNITEGQLA QGIADGANWH
FEINGQEFYA KGSNFIPPDT FWPRVTKEKM SRLLDAAAAG NQNMLRIWSS GAYLPDFIYD
LADERGVLLW SEFQFSDAMY PVDDAFLDNV AEEVVYNVRR VNHHPSLALW AGGNEIESLM
LPQTQDADPE GYPKYVAEYE KLYISLILPL VYQNTRSITY SPSSTTEGYI SVNLSAPVPM
TQRYEQLEPG SYYGDTDYYN YDTNVSFDYS IYPVGRFANE FGFHSMPSLQ SWQQAVDPDD
LHFNSTTVVT RNRHYPSEGF GETYNASRGM AEMTLGVERY YPIPENADPV ANFSAWCHAT
QLFQADFYKS QIQFYRRGSG MPERQLGSLY WQLEDIWQAP TWAGIEYDGR WKVLHYVARD
IYKPIIVSPF WNYTTGNFEV YVTSDLWESA TGTVNLNWLT LSGEPIPNNA GTPTTLDFAV
GAINTTRVYS TNINDLNLSN PKDSILVLSV SSEASLPNSN EPASLTHENH FTPAFPKDLA
LTDPELELSY DSESETFTVE SKSGVSLYTW LDYPAGLVGY FDHNAFILAP GQKKEIRFIV
QEDHSDGEWQ REVTVRSLWD QKARD
//
