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
//