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Database: UniProt
Entry: R5QVV9_9FIRM
LinkDB: R5QVV9_9FIRM
Original site: R5QVV9_9FIRM 
ID   R5QVV9_9FIRM            Unreviewed;       812 AA.
AC   R5QVV9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-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=BN747_01774 {ECO:0000313|EMBL:CCZ32930.1};
OS   Firmicutes bacterium CAG:646.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262995 {ECO:0000313|EMBL:CCZ32930.1, ECO:0000313|Proteomes:UP000018386};
RN   [1] {ECO:0000313|EMBL:CCZ32930.1, ECO:0000313|Proteomes:UP000018386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:646 {ECO:0000313|Proteomes:UP000018386};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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:CCZ32930.1}.
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DR   EMBL; CAZW010000039; CCZ32930.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QVV9; -.
DR   STRING; 1262995.BN747_01774; -.
DR   Proteomes; UP000018386; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 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; 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:UP000018386};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          191..287
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          657..741
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          746..812
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   812 AA;  95256 MW;  548223BDD29188DC CRC64;
     MKKQLIHEGW QMCCLEDQEW MSASVPGDVY SDLLANGKME DPFFKDNEYQ AKALMEKEYE
     YRTEFDFSEK EYEKARKIFL HFDGIDTLAD IYLNGTHLGE TISMHRIWEF PVEKVLKDGK
     NELRVVLHSP LKFMAEAFKK YGNIGNDDTI EGFMHLRKAH YMSGWDWGAC LPNAGIFRPV
     SLLGVEEARF DSVYIRQRHE NGQVALRPEI SMEIFEGAQE EFSYECKITH PDGTVQTVEG
     SPEEINILNP QLWWPNGLGE QPLYQVEVFL KKGGDVLDIW SGRIGLRTMT VRREKDQWGE
     SFAHEVNGKT VFAMGADYIP EDNMPGRTNP ERTRKLLEDC KRANFNAIRV WGGGYYPEDW
     FFDQCDELGL MVWQDFMFAC SVYELTPEFE DNIRHEFTDN VKRIRHHASL ALWCGNNEME
     MFVDERCWVT KDTEVRDYLF MYERIIPRML QELDPDTFYW PASPSSGGSF DKPNDPDRGD
     VHYWEVWHGN KPFSEYRKYF FRYASEFGFQ AFPSVKTLET VTDDPKDLNP YSYVMEKHQR
     NYGGNGKISQ YMQAAYRYPE NFNDFVYASQ LLQADGIRYG VEHYRRNRGR CMGAIYWQLN
     DCWPVISWSS IDYYGRWKAL HYYAKRFFAP VMVSCEEQSW MTAGANMNRQ HFEFEKSIRL
     NVANETLQDR KVLVRFAVRN AKAEILRQEE QWVEVKQLSS AWLDKVELPE IDCFSEYVSY
     EAEENGEIIS QGTVIFSYPK YFKYEDPKLT CRVDGDEIVV NASAYAKSVE IQNTEDDLVL
     EDNFFDMNGG ERRVRIISGK PEGLKLRSVY DI
//
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