ID A0A0D2E3S6_9EURO Unreviewed; 895 AA.
AC A0A0D2E3S6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN ORFNames=PV05_11090 {ECO:0000313|EMBL:KIW49410.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49410.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49410.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49410.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta-
CC mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}.
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DR EMBL; KN847323; KIW49410.1; -; Genomic_DNA.
DR RefSeq; XP_013309994.1; XM_013454540.1.
DR AlphaFoldDB; A0A0D2E3S6; -.
DR STRING; 348802.A0A0D2E3S6; -.
DR GeneID; 25332998; -.
DR HOGENOM; CLU_005015_1_1_1; -.
DR OrthoDB; 2504097at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt.
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; 2.
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 InterPro; IPR041447; Mannosidase_ig.
DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1.
DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT DOMAIN 236..337
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 738..824
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
SQ SEQUENCE 895 AA; 101928 MW; 31A749BE9AE66340 CRC64;
MQRPLREVRL CSIWSHGAIG DFVAIIFMAD NLSEWTSKLS RSCKHPMMAQ HRTRTPLSTW
TWRDCDGHGL SGRTQIPTNI HLDLLAAEAI PDPFIGKNEA DVQWVHSKTW AYKTTFEFQP
SRQHEFVDMV FEGLDTFATV KLNGREILKT DNMFISHRVD VTDLLRSDNE LEIVFASAYD
RGEASRSQKG HLLAWNGHYG RVYVRKAQYH FGWDWGPSLV TCGPWKPVYL DRYTHRIEDV
KVNVDLSEDC SEASVTVETT IEPCLPSQLS EVKLLDPDGT VLDTQKIQTN TANFKLTHPK
LWYPHTHGAQ PLYQINVIVR SESDKVLDSR KQTFGVRRIE LIQSPLQDGS TFYFKCNGVP
IFMGGSNWIP GDSFLPRMTA ERYQRWIDLA VRGNQNMLRV WGGGIYEDDA FYDECDRKGV
LVWQDFCFAC GQYPSDEAFR ESVKQEAIQA IRRLRHHPSL AIWAGNNEDY QIANEGLSHD
MKMLEDKWLE SSFGGRFIYE RILPDLVQAH SAGTLYWPGS PFGGVDNNSD RTVGDVHIWN
VSSGMLLPYQ RYPDIAGRFV SEFGMLSCPA LETVKSTFFG SSKDLHPQSE EFEFHCKASS
YEKRMFTCMG ENFRMSFNLP TYVYLTQLVQ SEAMGYAFRG WRRQFEQRKC GGALVWQTND
TWPVVSWAIV DYFERPKMAY YVISRALKPL VTGIARIEKI NPRPNQQHEA FVTGKTKADA
AGVIAHATPH IYPPKDSTYS VWVANATTTS TELSIRVRFI GVQSGLEVRP SMEQTIQAKA
TGTTEVMHGA TPKANEPIVL VSELFDLDGR LVSQEVDWPQ PLKHLTFPDR QLQVETSREG
VLEVSAAKPI KGLFFTNEGA EWSDNCLDVV PGQKLTVTAK GLKERPQWVY YGMED
//
