ID V2XNV5_9FIRM Unreviewed; 833 AA.
AC V2XNV5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=GCWU0000282_001031 {ECO:0000313|EMBL:ESL03864.1};
OS Catonella morbi ATCC 51271.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Catonella.
OX NCBI_TaxID=592026 {ECO:0000313|EMBL:ESL03864.1, ECO:0000313|Proteomes:UP000018227};
RN [1] {ECO:0000313|EMBL:ESL03864.1, ECO:0000313|Proteomes:UP000018227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51271 {ECO:0000313|EMBL:ESL03864.1,
RC ECO:0000313|Proteomes:UP000018227};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-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:ESL03864.1}.
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DR EMBL; ACIL03000007; ESL03864.1; -; Genomic_DNA.
DR RefSeq; WP_023353913.1; NZ_KI535367.1.
DR AlphaFoldDB; V2XNV5; -.
DR STRING; 592026.GCWU0000282_001031; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_3_2_9; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000018227; 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; 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, ECO:0000313|EMBL:ESL03864.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018227};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 256..305
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 677..760
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 764..814
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 833 AA; 97371 MW; C4D18761FF897B30 CRC64;
MTVQNLNENW KMREYHSAEY FDTKVPCSVY QTYLDHGLME DPYFRDNETK ALKMMEKDYE
FVSIFTPDEE IFKKPYVLLR FEGLDTIADI RLNDVYLGYA DNMHRAWEYE VKSLLREKDN
EIRILFHSPT KYIKEKDEKD GFWPIPTEAM RGTSHIRKSQ CMFGWDWGPR LPDAGIYRDV
KLLGSETERL DGVYIRQEHR DGKVILSAEI ELKCMDSRFP LCFGEDKELI GNRNIDAKIS
ILNPQGMLTG VIEAKHGEKI SEIEIAEPQL WWPNGLGEQP LYTVKTELLR DGEIIDQTEK
RIGLRTLTIR REKDEYGESF AQEVNGIIYF AMGADYIPED CILSRINAAR TRDLLGQAVA
ANHNSIRVWG GGYYPDDFFW DICDELGLVV WMDFMFACGV YGLTDPEFER NMTEEFIQNV
KRIRNHASLG LWCGNNEMES FYHANILGFD KQKKFAADYI KLHEYIIPRV LREHDPETFF
WPSSPSSGGG FEDTDSPDKG DVHYWDVWHG NKPFTEYRKF RFRYLSEFGF QSFPSIRTVE
SFTEPEDRNV FSWVMEKHQR NAAANGKIMN YMEQTYLYPT DFETLLYASQ LLQADAIRYG
VEHFRRNRGQ CMGTIVWQLN DCWPVASWSS IDYYGRWKAL HYYEKRFFAP LLLSCEEEGA
LSQDPNPNAE PYELKKSIRL CVSNETMSPE KVRVFWELRD NTSAVLRSGQ QDARVDAMSC
VWLEREQFDD ADEFSNYVSY RMEKDGEEIS GGSVLFTVPK FFRLADPKLR VSVDGDEIVV
SSENYARAVE IRNKDDNLIL SDNFFDMNAG KKRVKILRGE PDMLEVRSAY NIR
//
