ID R9L8Z7_9BACL Unreviewed; 882 AA.
AC R9L8Z7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=C812_03238 {ECO:0000313|EMBL:EOS54841.1};
OS Paenibacillus barengoltzii G22.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1235795 {ECO:0000313|EMBL:EOS54841.1, ECO:0000313|Proteomes:UP000019598};
RN [1] {ECO:0000313|EMBL:EOS54841.1, ECO:0000313|Proteomes:UP000019598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G22 {ECO:0000313|EMBL:EOS54841.1,
RC ECO:0000313|Proteomes:UP000019598};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Paenibacillus barengoltzii G22.";
RL Submitted (APR-2013) 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:EOS54841.1}.
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DR EMBL; ASSZ01000028; EOS54841.1; -; Genomic_DNA.
DR RefSeq; WP_016313659.1; NZ_KE159654.1.
DR AlphaFoldDB; R9L8Z7; -.
DR STRING; 1235795.C812_03238; -.
DR PATRIC; fig|1235795.3.peg.3205; -.
DR HOGENOM; CLU_005015_3_2_9; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000019598; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; PF02837; Glyco_hydro_2_N; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 70..138
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 210..324
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 696..794
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 798..864
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 882 AA; 99816 MW; 378264D54177CD95 CRC64;
MILSGPWKLQ HFEVGEKPPL ELAAPGLDDR FWVETHVPSD VHSTLLARGL IDSPYYGHND
AKCRWIERKE WWYRTTFELE ALPGETERIE LVFEGLDTYA SVFVNGHEIG SASNMFRCYT
FDVTRIVREG RNTIAVRFDP LYLHHRDKEQ LEWSSYTKER PWIRKAAMNF GWDWGPRIVT
TGIWGPVRLE RRRLAKLTSV YAATISATAE EAVIQISAEV EAYRSGTAAV AALRLLDAEG
EEVASATLSM LDAEQPLIGG QAALRQAFPN AIRTKGAASA ELRVTKPRRW WTHDLGEPYL
YTLEVTLLAG DEEVDRYEQP FGIRTLELSL EQPDGSPSFA FILNGIKVYA KGANWIPADH
LIGSIPESTY RGLIELAVEG HMNMLRVWAG GIYEKEIFYE ECDRRGVLVW QDFAFANALF
PDFNHDFMDN VRQEIIDNVK RLRNRASLAL WCGNNEIDWL YDMKSAGGEI TGDFYGESIY
HELIPGLLAE LDPYRPYWPS SPYGAQDGYD ANDPNQGDRH NWQVWHGSVY PRMQGEKPLL
DYSIQGVTFK NFKQDFALFS SEFGMHASAN RYTLEKNIPE GQFTWGSAEM AYRNKDTNHR
KGILLMEGYT GIPRDIEEYM NFSMLTQAEG LKYGIEHYRR HRHRNSGALV WQLNDSWPGT
SWSMIDYELL PKASYYYGKT FFHPVLLSLE HEPGEPLHVW VVNDTLERLE GTMIVTVHPL
VQQGGAAKTA EGTRDGGIRQ FTLPAVVPPQ TAVRLGRLEE AEALAGLAPE EVLVELSAAG
FSAPVNRYYL RDPKELRLPA AELDVQVDEA EQTVTVTASG GTAARLVKLE LPLGGVRYSD
NYFDLLPGES RTVRLRHPDG LSLPWAALRV GALNAAVWLG KR
//
