ID A0A176UAJ8_9FIRM Unreviewed; 850 AA.
AC A0A176UAJ8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=HMPREF2738_00084 {ECO:0000313|EMBL:OAD89877.1};
OS Clostridiales bacterium KLE1615.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD89877.1, ECO:0000313|Proteomes:UP000077212};
RN [1] {ECO:0000313|EMBL:OAD89877.1, ECO:0000313|Proteomes:UP000077212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1615 {ECO:0000313|EMBL:OAD89877.1,
RC ECO:0000313|Proteomes:UP000077212};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:OAD89877.1}.
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DR EMBL; LXPQ01000008; OAD89877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176UAJ8; -.
DR PATRIC; fig|1715004.3.peg.80; -.
DR Proteomes; UP000077212; 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:OAD89877.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077212};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 224..318
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 673..760
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 763..847
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 850 AA; 98241 MW; 654AEBFB62B939A3 CRC64;
MTMERVNLQE DWRFAEVNSD EWTPVSVPGT VLSGLLEAGK MQDPYYRENE YEARELLAKD
YVFETDFCIS EEQLNKKHCV LVCEGLDTLA DVYVNEKLVG KVDNMHRTWR FDCKDALQKE
NHLRIYFHSA LTYIREHEAT PGKEITYEPT GGILGNQYIR KAHSMFGWDW GAQLPDIGIW
RDLYLECYNA GRIEDVVICQ KHTWKERPQM GELSQEEYIE AVEQSDTVSL SVEVKPEQDT
NLENTKVIVT LTDPKGVQLE QVVLPIIKEA VCAEILVAQP KLWWCNGLGD QPLYKVQVSL
VDNNQCVLDS KEYSIGLREL TVSTKKDEWG NEFAFVINGI HIFSMGADYI PEDCIYPWIT
KERIEALIRS SVKANYNMLR VWGGGYYPSD TFYDLCDQYG LIVWQDLMYA CNVYDFTEEF
EKNICQETVD NVRRLRHHAS LGLWCGNNEL ESAWDHWGIS ETHSPLLKGD YIKQFEYVLP
KVTKEEDSNT FYWPSSPSSG GCFDKPDDHD RGDCHYWDVW HGMKPFSDYR SHYFRFCSEF
GFQSFPERKT IDTFALPQDC NIFSPVMESH QKNGTANGKI LYYISENFRY PKDFDSLVYV
SQVLQGIAIK AGVDHWRANR GRCMGALYWQ LNDNWPVASW ASIDYFGRWK ALHYMAARFF
APKAGYIYTE GTKAVISAAN ETLENQSLNV TVRIRDVELN VLFEETVETT VKAQSSIHVL
ERDFADVIGS KKRRVFAEAV YTWQDGTTST EAESFVPYKH MDLLQPQIET SVTEKDGTIE
IQISADCFAP FVWLETEEDV IFSDNCFDLT SEETKTIYIQ KEDVLSGKAL SADNVRKTLK
IRSLRDTYEQ
//
