ID A0A1M5WAG9_9CLOT Unreviewed; 783 AA.
AC A0A1M5WAG9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN02745207_02767 {ECO:0000313|EMBL:SHH84492.1};
OS Clostridium grantii DSM 8605.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121316 {ECO:0000313|EMBL:SHH84492.1, ECO:0000313|Proteomes:UP000184447};
RN [1] {ECO:0000313|EMBL:SHH84492.1, ECO:0000313|Proteomes:UP000184447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8605 {ECO:0000313|EMBL:SHH84492.1,
RC ECO:0000313|Proteomes:UP000184447};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQXM01000016; SHH84492.1; -; Genomic_DNA.
DR RefSeq; WP_073339012.1; NZ_FQXM01000016.1.
DR AlphaFoldDB; A0A1M5WAG9; -.
DR STRING; 1121316.SAMN02745207_02767; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000184447; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
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; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 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:UP000184447};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 78..137
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 194..305
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 356..448
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 665..744
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
SQ SEQUENCE 783 AA; 90577 MW; A8C83E7FFD9DA723 CRC64;
MSRIVLDLSN EKWQCEHIRP GQGIKEEFHK IPCERQGSAF NWNYVKIPGD VYTDLQRVGE
VEDPFFGQNM HKMKWVQEQE YWYMCKFNVP VEMEGKRINV LFEGVDYSCN VWFNGHELGG
HEGMFSQFAF EISPFVNFAQ WGGGSNILLV RLDPPPRNFE RVSGMKFNYN GDYHTGLVPF
GIWRPIKLVA TENVKIENTR IESYVNNKNA RVSIDVLVDN LVAKSENMTV ELTIEGKNCD
TKTITKSIDT LISSGENKIS FDMDIDNANL WWPWDMGEQN LHIATIKILK DGLLVDEVVE
IFGIRQIEMA MNPGYEKEEA ENPWTFVING TKTYLRAACW GGQPSLLYGK NSDEKYEKLL
NMVKEANVNH LRIFGWHPPE VPAFYNLCDE LGITVWTNFT FSTNVIRKEL PFGDAMINEC
MEIVKDRRNH PSAIFWMGGE EVSFTDAHAE SGNKKLMSMI GEEIKRYTNT PYGLASPLSN
ETGIKMGYKT KESQHANEHY YGAGHIFMEE YYPSLDCCIV PELTAASAPS VESLKKFIPE
DELWPMGMSW AYHWADIDYL KILNVEVFDD VKMGSLEEFV EATQLAHGII LQYALEFYRR
RKPYNSGVAL CHFITHWPDI KWGLVDYYGE KKLCFDYVKR TYSPLLVSLA YDKRRWEEKE
EFKSAIWVVN DYYKSFENLT IKYKVTDENS KVIAEKIESI QKVESASSKE FINIACETPK
GKTFNIAIEL LNDKNEVIAE NEYTLLIGSQ SKAKAICKEM RLDADKRQIE MPGFYRYFPE
KWV
//
