ID A0A150VI40_9PEZI Unreviewed; 833 AA.
AC A0A150VI40;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=M433DRAFT_548 {ECO:0000313|EMBL:KYG50121.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG50121.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG50121.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG50121.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
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:KYG50121.1}.
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DR EMBL; JPDO01000009; KYG50121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VI40; -.
DR STRING; 766039.A0A150VI40; -.
DR Proteomes; UP000075602; 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, ECO:0000313|EMBL:KYG50121.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602}.
FT DOMAIN 192..295
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 673..760
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
SQ SEQUENCE 833 AA; 95775 MW; 17CFC763D5828906 CRC64;
MSTAQTLESG WQFKQTDTDE WLPVARVPTN VHLDLINNKR IEDPFLGFNE LKCEWVGERS
WTYRVTLPTL PPLKDGAKHV LAFDGLDTFA TVKLNEKVIL ESDNMWIMHR IDVTSILELA
KENILEIEFK PALLEARKIK ESHPEHKWLG FNGDMARLAV RKAQYHWGWD WGPVLMTCGP
WRSVRLETYQ ARVADLRIDY QVDSSFKKVT GSITATIEGN SGKAVNFSAK LGDTVVFKGT
TELDNNAKAK VEFHVNEPKL WYPHGYGEQP LYTVTATVTN GEYDLHSLSK RTGFRKGELI
QEPDEVGKTF YFRFNGVDVF CGGSDWIPAD SFTPRITPEK YRKWLEMMVD GYQVMIRVWG
GGIWEEDVFY DICDELGVLV WQDFMFGCGN YPAYPEMLKS ITDECVCQTK RLRHHPSLAI
YAGNNEDYQV QETYKLTYNY EDKDPESWLK TDFPARYIYE KLLPEVVAAH SPHVPYHPGS
PWGDGKISSD PTVGDMHQWN VWHGTQEKYQ IFDTLGGRFN SEFGMEAFPH IDTIKYYVTD
PSQLYPQSHM IDFHNKADGH ERRIATYLVE NFRTQTDLEK FIHLTQLSQA EALMFGYRGW
RQQWGKKRFC GGALVWQLND CWPVTSWAIV DYFLRKKPAY YAMRRVLAPI AVAVKRAHHD
WSVVHARPAK SSHYECWVAS SKVEEITATV ELRYISISTG KDIKDKIVRS GVKIAPNGTT
EIFHGMIDNE KEEPHVLAAR IWVDDEIVSR DVDWPQPLKY LDFSDRGVEV SPNGKTISVR
ARKPTKGLVF EEREGVLVHD SALDVVPGDE QIVHVRGLAP QDNPLKWTYY GAP
//
