ID B5XRT8_KLEP3 Unreviewed; 732 AA.
AC B5XRT8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 OrderedLocusNames=KPK_3086 {ECO:0000313|EMBL:ACI10783.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI10783.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI10783.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI10783.1,
RC ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI10783.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XRT8; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; kpe:KPK_3086; -.
DR HOGENOM; CLU_005015_5_0_6; -.
DR BioCyc; KPNE507522:GI0B-3073-MONOMER; -.
DR Proteomes; UP000001734; Chromosome.
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; IPR006103; Glyco_hydro_2_cat.
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; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
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:ACI10783.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..732
FT /note="Beta-mannosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002838504"
FT DOMAIN 194..304
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 316..472
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 643..720
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
SQ SEQUENCE 732 AA; 82704 MW; CDE8F23E8F624CDE CRC64;
MIVKRLLLLM VCLPLAHAGS APVTWSLAGQ WRVHDANDSA FDGAQASDGD WRTLRVPANW
YSAGYDHQGA LWYRHQFTLH GLSPDAMATL VFDGVDYFAE VALNGKTLAR HEGYFQRFPV
DISGAVRRHN QLAVRVDSPY EDPQKIWPLH KTLMKGILNQ HDTRPGGAWS VQGQDANSGG
IWAPVKLHLS RGVTIDEVIL RPDWQQGLEQ PMLRAEIRYR AVTPGPVTLR LTATPDNFSG
PRFHQAFAVT LEKTAGVLHV SLPMPSAKLW WPVGAGKPNL YRVRATLTDN RGMMDTAVTR
TGLRKVEALT DNQGWRINDR RLFIKGSNYI GSPWLSTMTR KKYRRDFRLV TAMNANAIRV
HGHVAGRALY EVADEMGLMI WQDVPLQWGY DDSAAFAENA VRQTRAMMDQ FGNSPAIIVW
GGHNEPPWNS PWMEKRFPDW HKTLNQTLTQ RVGDALAEDT SRIVHRFSAV EEHYWAGWYF
GTLRDLLAPA KTGIITEFGA QALPRLSTLK TIIPAHLLWP KTTAADDPGW VRWKYHNFQP
FQTFKFAGIP RGNNIQEMIE NTQAYQARLV ALAAESYRRQ RYQPVTALFH FMFVETWPSI
NWGVVDYLRQ PKAGYYALQR AYQPILPSIE PVTASWRKGS PATVRLWAIN DTWAACENCR
LTWQVRQNGQ MLAQGETSLT LPPDAGQMVR ELTVTPAGPQ PVTIDYRIDN RRGKRVGANQ
HTEPVAAAQA GR
//
