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Database: UniProt
Entry: A0A231R3K5_9BACL
LinkDB: A0A231R3K5_9BACL
Original site: A0A231R3K5_9BACL 
ID   A0A231R3K5_9BACL        Unreviewed;       823 AA.
AC   A0A231R3K5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=B1A99_28995 {ECO:0000313|EMBL:OXS53690.1};
OS   Cohnella sp. CIP 111063.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1955714 {ECO:0000313|EMBL:OXS53690.1, ECO:0000313|Proteomes:UP000215193};
RN   [1] {ECO:0000313|EMBL:OXS53690.1, ECO:0000313|Proteomes:UP000215193}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 111063 {ECO:0000313|EMBL:OXS53690.1,
RC   ECO:0000313|Proteomes:UP000215193};
RA   Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT   "Cohnella sp SGD-V74 (T) CIP 111063, whole genome shotgun sequencing
RT   project.";
RL   Submitted (MAR-2017) 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:OXS53690.1}.
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DR   EMBL; MWSG01000024; OXS53690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231R3K5; -.
DR   Proteomes; UP000215193; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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; IPR006104; Glyco_hydro_2_N.
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; PF02837; Glyco_hydro_2_N; 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:OXS53690.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215193};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          61..128
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          188..291
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          645..735
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          740..821
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   823 AA;  95458 MW;  192C5E7696A27A73 CRC64;
     MRELTLNGEW EMKRTDEAEW IGATVPGSVF QDLLAAGRME DPFFRDNEYE TLELTKFDYE
     YRRSFFVDAE LLKHERVLLR CEGLDTLCEV SVNGRLVLQT NNMHRTYEAD VKETLSEGRN
     DIVVVIRSAT NYVLARDREY HLTSCADAVP GISHLRKAHS MFGWDWGPKL PDMGIWRGLS
     LLGCDGGRIE DVYVTQRHED DRVGLEIDAT LERWSEAAEL RLLATIDTPD GKRLEVSAER
     AANTNRLTVD IAEPKLWWPN NLGDQPLYTL RIRLLSGERE LDERTMKLGL RTLRVQQTPD
     QWGESFAFEI NGHEIFAMGA NFIPEDNVFG RRSEERMERL IRSCVEANYN CIRVWGGGYY
     AEDYFYDLCD RYGLIVWQDH LYACGAYDFN DEFKENVRLE TVDNMKRIRH HASLGIWSGN
     NELEYAWAYW GWTERYGEKL RDDYLEQFER FLPELSKSLD PNTFYWVSSP SSKGGIDDPN
     NEHVGDMHYW DVWHGRKPIT EFRTLFPRFM SEFGLQSFPS LRTVETFTLP EDRNIFSRVM
     EAHQKNGTGN EKIMYYVSEY FKYPKNFETL LYVSQLIQAE GMPVGVEHWR RHRGRCMGAI
     YWQLNDIWPG ASWSSLDYYG RWKATHHAAR RFFSPVLASA CEEGTKVSLH VTNETLQPIA
     GRLRWRLLDH RSAPIAAGEA EAELDALSTR EVVVLDFAET LSDSRQLRRS YLAFEWLADG
     RTISSGTVLF VKPKHFDFLE PGIRLDATEE DDRFVVTATS RAFARFVLLE LDGADAEWSD
     NVFDLSADRP HVVTVRKAGL SEPLDLKAFR ERLKATSLFD TFE
//
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