ID A0A150AIC6_9BACT Unreviewed; 861 AA.
AC A0A150AIC6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=AVL50_12330 {ECO:0000313|EMBL:KXX69676.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX69676.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX69676.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX69676.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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 -!- 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:KXX69676.1}.
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DR EMBL; LQAQ01000061; KXX69676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150AIC6; -.
DR STRING; 1775430.AVL50_12330; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000075267; Unassembled WGS sequence.
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; 3.
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; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000075267};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 221..326
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 686..778
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 781..860
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 861 AA; 100108 MW; 52DCD86FC6672C71 CRC64;
MKNITYLTYA FLSLLILSCS TDWESQEQLK KSYPLHSDWE FKQANKEQWY PATVPGVVHT
DLFQNKLIED PFYRQNEKDL QWIEEEDWVY KTTFDLPTSF KENQHFALNF EGLDTYADVT
LNGKKVISSD NMFVGYNKEV TSLLKEKGNV LEVYFHSPIK ITKPLREQAG FEYPADNDAR
EEKYSIYSRK APYSFGWDWG PRFVTSGIWR PVELVVWNSA QINDVHLQQV SLTEEKAKLK
ATVEVKSSVV GDANIRLINN SSTFSSQEKK VMLNKGLNVI ELEAEVENPE LWWPNGLGEQ
TRYEIITQLN VDGNFVDQES HKIGFRTVEV INEPDSIGES FFVKVNGQPV FMKGANYIPQ
DSFLPSVTKD RYDWMIESMV RAHMNMVRMW GGGIYESDYF YDQCDEKGLL VWQDFMFACT
MYPGDKDFIR KVKEEAAYNI KRLRNRPSLA LWCGNNEVGV AWDNWGWQDS YGWSEEVQAK
LLEDYNRLFK EVLPEMVKTY DEGRFYYPSS PISNWGNLED FTIGDNHFWG VWHGKYPFES
FKEYVPRFMS EYGFQSFPSF KAIKKFTIEE DWGLETDVMN THQKSYTGNG LIKVYMERDF
NVPTDFEDFV YVGQLLQADG MRQGFEIHRR RMPYCMGTLY WQLDDCWPAA SWSSIDYYGE
WKALHYAAER AFEPQLISTD IEDELLTVWL VNDEWKEIGA TLNVKWNTFD GKELVKKSLP
IKVDGNTSKV VLESTLEELL GRKSTLKERK SMYLTLEAED ANGKVIAKNY AFFFKPKDQI
LPKANIKTTV VEEGNTLKIK LKSDVFAESV ALSLAGEATA HFSDNYFHLE ANQEKVITLE
RTTINAEELK KALEVKCLNN I
//
