ID B9WL84_CANDC Unreviewed; 815 AA.
AC B9WL84;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN OrderedLocusNames=Cd36_27860 {ECO:0000313|CGD:CAL0000164486};
GN ORFNames=CD36_27860 {ECO:0000313|EMBL:CAX39789.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX39789.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX39789.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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};
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DR EMBL; FM992695; CAX39789.1; -; Genomic_DNA.
DR RefSeq; XP_002421845.1; XM_002421800.1.
DR AlphaFoldDB; B9WL84; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GeneID; 8049597; -.
DR KEGG; cdu:CD36_27860; -.
DR CGD; CAL0000164486; Cd36_27860.
DR VEuPathDB; FungiDB:CD36_27860; -.
DR eggNOG; KOG2230; Eukaryota.
DR HOGENOM; CLU_005015_1_1_1; -.
DR OrthoDB; 2504097at2759; -.
DR Proteomes; UP000002605; Chromosome R.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
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 PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CAX39789.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAX39789.1}.
FT DOMAIN 189..285
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
SQ SEQUENCE 815 AA; 95037 MW; D168B894097D5FE7 CRC64;
MAVDLTNWQF RQISNHIKSP LISNQWYDTK NFSSHQIHVD LLYANIIPDP FIDDNEIHVQ
WIGELDWQYR CIFDVPGTSI GNASLIFEGI DTFADIQLNN KTILTTENYF QKHIIPITVN
SHNELIITFN SSLKVGQELE QEYGKLQVWN GDSSRVYVRK PQFQYGWDWG PTLNTCGFES
IKLITEKDHV NDFFIRYNLN QEMNIAELSI EIDFLFDDYP ESLEIKIKDD ADVVIDSIVP
TSSITNYNIS NVKLWYPRNQ GEQPLYTFSL FVNGMCKTTL KVGFRKIELV QLNDKYGKSF
YFKINNIPTQ IFGTNWIPAH SFQSQLTDLE YQQWINLIVN GGYNLIRIWG GGQYEKDILY
SLCDEVGILI WQDFMFACGI YPQTIIESVT QEVEDQLIRL RQHCSIVIYA GNNEDYQIAE
SINLDTNNFT QFPAKHIYEH IIPAKINKLC NLTPYHYGSP YSDHSHKSSN PTIGDLHQWN
VWHGTHEPYQ NWPQLSGRFV SEFGMLSYPS LNTLAKYINE SQLSINSTLL NFHTKAAGKE
QLNNYLWNNF PKPKSLEISH YIYLTQLLQS EAMSLAYRYW RQNWKDYKTG GIIMWQLNDC
WPSISWSSID FLKVPKLAYY GVKREISQIG IACRRFQIKQ QTYKQQNVFE VKQCLDIWGV
GEFSKIDVEI EFYNEHGELY FSKSINSCVF LKNKVNMVAE KLCFDNLNDN SIIYLKLIQN
GRTIAQSSDW PQPLKKLSWN QMATNITLEY LGEGNFQVST TKPVKGLEFY FDSIDNYLFD
DNGIDLFPND PQIIHVNGFD NLDVSKIRYR HLVSI
//
