ID A0A178ZWN1_9EURO Unreviewed; 853 AA.
AC A0A178ZWN1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AYL99_02632 {ECO:0000313|EMBL:OAP63405.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP63405.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP63405.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP63405.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAP63405.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVYI01000002; OAP63405.1; -; Genomic_DNA.
DR RefSeq; XP_018696772.1; XM_018834148.1.
DR AlphaFoldDB; A0A178ZWN1; -.
DR STRING; 1367422.A0A178ZWN1; -.
DR GeneID; 30006802; -.
DR OrthoDB; 2504097at2759; -.
DR Proteomes; UP000078343; 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; 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 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:UP000078343}.
FT DOMAIN 206..313
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 691..778
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
SQ SEQUENCE 853 AA; 97344 MW; 3554DF6553CC6791 CRC64;
MGDMSGVDDM LAPVEVVDLS VGWSFKQSDD VGENAWCPVK KLPSTVHQDL IDNKKLDNPF
VGFNEIKAEW VGLKSWTYRT RLARPFVAQG SKVVLAFDGL DTFAHVKLDG KTILRSDNMF
LPHRVDVTEA IQSRSDHSLE IEFEPAFLKA REIKDQHPEH KFICFNGDSA RLAVRKAQYH
WGWDWGPFLM CAGIWKPVRL EIYSIRIADL RTDVVLSDDY KLATIHASAD VEGLEAQYGH
VEAHFTVSLG DRQILSRQAN VVLGKKTAAE LQVSDPQLWM PNGYGQQPLY TVSVTISIEG
TVLHKESRRI GLRKVQLVQE PDSHGKSFYF RVNDVDIFCG GSCWIPTDSF LTNVTPEKYR
AWIELMVPAN QKMIRVWGGG IYEHDSFYDA CDELGIMVWQ DFMFGCGNYP CFPAILKSIE
AEAVANVRRI RHHPCVVIFA GNNEDYQVQE SAHLTYDYED KNEEHWLKSD FPARYIYESL
LPKVAAAEAP WIPYHPGSPW GDGKISSDPT VGDMHQWNVW HGTQEKYQIF DSLGGRFNSE
FGMEAFPHIA TIKSFVEREE DLYPQSHVLD FHNKADGHER RIATYLVENV RTVTKLEAYI
HLTQLIQCEA LMFGYRGWRK QWGDDRHCGG ALVWQLNDCW PVTSWSIVDY YLRRKPAYYA
MARVLAPVAV GIRRSHHDWS VTHAREPRTQ DWELWVVSAK LTEITADVEV RFVSVRTGLE
IKDKMVKKGI KIKANGTTDV LKGQVDNVQE EPHVLAARIW VDGTLVARDT DWPQPLKYLQ
FPDRNVKVEV VGDEMHVSAD RPVKCLVFEE REGCHLSDSA IDLVPNDQQI IRVRGLKAGE
PPLDWTYLGA GEQ
//
