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Database: UniProt
Entry: R5Y9Q3_9FIRM
LinkDB: R5Y9Q3_9FIRM
Original site: R5Y9Q3_9FIRM 
ID   R5Y9Q3_9FIRM            Unreviewed;       817 AA.
AC   R5Y9Q3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN   ORFNames=BN695_01568 {ECO:0000313|EMBL:CDA13347.1};
OS   Anaerotruncus sp. CAG:528.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=1262700 {ECO:0000313|EMBL:CDA13347.1, ECO:0000313|Proteomes:UP000018024};
RN   [1] {ECO:0000313|EMBL:CDA13347.1, ECO:0000313|Proteomes:UP000018024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:528 {ECO:0000313|Proteomes:UP000018024};
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:CDA13347.1}.
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DR   EMBL; CBBE010000059; CDA13347.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5Y9Q3; -.
DR   STRING; 1262700.BN695_01568; -.
DR   Proteomes; UP000018024; Unassembled WGS sequence.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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; 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; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDA13347.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018024}.
FT   DOMAIN          59..127
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          627..704
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          718..784
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   817 AA;  93060 MW;  BFEF85E5332C7FE4 CRC64;
     MERMSLAGKW ILHMDKQDRD YEADVPCSDY GTLLKNGAID DPFYKTNEHK CLFIAETGKS
     FKRSFKISQE QLEYRKALLR CQMLDTLAQI YINGQMADIS SNAYVCSETN ITDYLHEGEN
     TIEIHFLSPI EYVKSKQSEA PLPPNANGID GVPYIRKPAC HFGWDWGINM PVSGIFGNIE
     ILFYNNEIRD FWVRQEHSEN GEVKLYIKAN KALDSSGQII TPSGESIAFG IEKGNACVTI
     KNPELWQTRE LSGKEKQPLY TVCVAGIKKR IGLRTIVLDR SEDEYGSNFR FILNGVPIFA
     KGANVIPPDA MADRIGKKTA EKIVSDAVHA NFNMLRIWGG GYYGSDELYD LCDEYGILVW
     QDFMFACLMY PFYDEVFLKN VLDEVKYNVR RISSHPSLAL WCGNNEIEFM FQHLPSTLKI
     VKWYKEFFYE ILPGELRRYD KDTPYIETSP IGSGFRKDIT ADKCGDTHMW HVWHGSKDLS
     YYGKRYTRFC SEYGMESFPS EDCILQFATQ KDMQLKSDVM QSHQKCASGN DKMLFYLYEK
     FNKPAKFADL IYLTGLTQAE CVANGAEHWR RNKGRCNGAL WWQMNDCWGA PSWSSVDYFG
     KWKPLMYAGK RIFAPITISL RQADGGIELY VLNGTQKNEE YTAVITFKDF TGKELRSKSL
     LIKSHAGESQ KAFYISAGGL KKASCFAQAE LLKGGKTVLS RTAVLLPERK LKLQHAKITL
     YLSGNEMTLE SNTFARSVFV DIKGESAPLS DNCFDLVPGE KKTIRLEKDC KIDPKSISVK
     CVNNITYAGG DAERIRFRMA FSAQPMNIAN KIYYSIS
//
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