ID A0A219AR49_METCM Unreviewed; 878 AA.
AC A0A219AR49;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=VFPPC_17579 {ECO:0000313|EMBL:OWT43258.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OWT43258.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OWT43258.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OWT43258.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(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 -!- 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 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:OWT43258.1}.
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DR EMBL; LSBJ02000002; OWT43258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A219AR49; -.
DR STRING; 1380566.A0A219AR49; -.
DR OrthoDB; 2504097at2759; -.
DR Proteomes; UP000078397; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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:SF1; BETA-MANNOSIDASE; 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; 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:UP000078397};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 196..301
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 698..797
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 812..863
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 878 AA; 100400 MW; DE882BE1C8AA8114 CRC64;
MAHTRVQLTS GWTFKQQEWS SEEWLPVSQV PSQIHMDLLA HKKIPDPFVD INERAVQWVG
DKVWQYKVSF PTPKASSGDL TTDLVFEGLD TFATVALNGK EILKTDNMFV SYRVNISEHL
KHDGDNVLEI EFDSAWIRGR ELVKEHSHEH NFLVRQTEAG RVAVRKAQYN WGWDWGPILM
TAGPWKPVYL EQYTARLDDV WAQNEVASDL KTCSGTIYAN IAGQVHTNDK LAVSLTLDGK
NIIQEQVTIP NNGKVSVPFK IADPQLWYPL NYGPQTRYNL QATIVRNDIE LHATFKLIGF
RRTELVQEPD AHGKSFYFRI NNVDVFGGGS CWIPADSYSS AISPKRYYDW IKLMAEGNQV
MIRVWGGGIY EDDSLIDACD ELGVLVWHDF QFACASYPTY ASYMKTLEVE VRQHIRRLRW
HPSVIAWAGN NEDYQVQERY KLDYDFENKD PDSWLKSTFP ARYLYEHFLP ELVKEEDPFM
IYHPSSPWGD GKPTADPTVG DIHQWNLWHG AVNKYQEVSL LGGRFISEFG MEAYPHLSTV
QRMTTHPSQL YPGSMTIDFH NKGIFNERRM TTYVSENFRL KYDLPSYIHL TQVVQAEAMR
FAYKTWRRDW GTAGDRKCGG VLVWQLNDCW PTMSWAVVDY YLVKKPAYYA ISRALRPLDI
GVTRTYHDWT QTGYYIDENS KLCTGQVDQT LPARQSAFDV WIASSNVQPV DAQVTVRFIS
IRSGKDVTDS ITESITATPN ATTTVFSNKP LKPSIPHHDD YTVPFDVTQY DPYVVYTTLS
VNGSVVATDT AWPDPIKFLD MPDRGISFSI TSKNQVTVSA DRPTKGFVFE EVEGMKLSDN
GFDIMPGDKH DITVDGPVSA EKLRWTYIGA DDASLEIK
//
