ID K9E9G1_9BACE Unreviewed; 865 AA.
AC K9E9G1;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HMPREF9447_05021 {ECO:0000313|EMBL:EKU87562.1};
OS Bacteroides oleiciplenus YIT 12058.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=742727 {ECO:0000313|EMBL:EKU87562.1, ECO:0000313|Proteomes:UP000009872};
RN [1] {ECO:0000313|EMBL:EKU87562.1, ECO:0000313|Proteomes:UP000009872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12058 {ECO:0000313|EMBL:EKU87562.1,
RC ECO:0000313|Proteomes:UP000009872};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., 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 Bacteroides oleiciplenus YIT 12058.";
RL Submitted (SEP-2012) 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:EKU87562.1}.
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DR EMBL; ADLF01000024; EKU87562.1; -; Genomic_DNA.
DR RefSeq; WP_009132400.1; NZ_JH992946.1.
DR AlphaFoldDB; K9E9G1; -.
DR STRING; 742727.HMPREF9447_05021; -.
DR PATRIC; fig|742727.4.peg.5126; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_3_2_10; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000009872; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..865
FT /note="Beta-mannosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003929407"
FT DOMAIN 223..329
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 692..780
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 787..861
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 865 AA; 100355 MW; 69E6861969771D32 CRC64;
MNTKVKTRTW IALLNLLFLF TTVNAQPVRQ YLHEGWNFRQ ARGTNWYEAT VPGTVHTDLM
DNKLIDDPFY RLNERGVQWV DKEDWIYRTT FEVTPELLAK KNIVLHFEGL DTYADVTLNG
KKILSADNMF CEWQADVRSL LKEHGNELQV YLHSPIKIAM PKWETVPFQY RSSNDQSENG
GLLNRKVGVF VRKAGYHFGW DWGPRLVTSG IWRSVSLEAW DEARINDVFY NQQSVTAQQA
VVDVTVEVLA DEEIEAKVAV INHTDNRTEC QKLIRLNKGL NKVPVSFTMK NPRLWWTNGL
GEPFLYNFAT TLELDGKQID ITEEKLGIRS LKVITAPDKY GESFYFELNG KPLFAKGANY
IPCDNFLTRV TDSIYEKTIR DAVSANMNML RVWGGGVYEK DIFYDLCDKY GILIWQDFMF
ACSVFPAEGE LLENIRREAI DNVRRLRNHS CIALWCGNNE CLDAWFNWNW KNTYDKQNPA
YSDIIWKQFK DQYFVTLPAV VEEFHPGACY RKSSPYSDDK GTRNHTVGDM HYWEVWQGLK
PLSEFNHERS RFFSEYGFQS FPEFESIKRY APLPEDWKLT SEVMMSHQRG GTAANKRIND
FLLSEYRQPK DFRSFTYMSQ LLQADAMKMA MEAHRRDMPY CMGSLVWQHN DCWPVASWSS
RDYYGRWKAQ HYFTVKSFAD LLVSPIEKEN ILQIYMVSDR LKSTSGKLTV CVFRLDGSGV
VKEFKKQITV PANTSTVVWK EAVDELLNGE KKEDVVVHVF YKDKTGTEYT NNYFLAKQKD
MHYAAARINK DFVPTEGGYE VTLSCDVFAR GVFLSLQEDI DNFISDNYMD ILPGKPVTVK
VTTELPSLQF AEKLQVASFS DAVEQ
//
