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Database: UniProt
Entry: S0J3L4_9FIRM
LinkDB: S0J3L4_9FIRM
Original site: S0J3L4_9FIRM 
ID   S0J3L4_9FIRM            Unreviewed;       835 AA.
AC   S0J3L4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=C805_00929 {ECO:0000313|EMBL:EOT26827.1};
OS   Eubacterium sp. 14-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235790 {ECO:0000313|EMBL:EOT26827.1, ECO:0000313|Proteomes:UP000014176};
RN   [1] {ECO:0000313|EMBL:EOT26827.1, ECO:0000313|Proteomes:UP000014176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14-2 {ECO:0000313|EMBL:EOT26827.1,
RC   ECO:0000313|Proteomes:UP000014176};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Eubacterium bacterium 14-2.";
RL   Submitted (APR-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:EOT26827.1}.
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DR   EMBL; ASSS01000005; EOT26827.1; -; Genomic_DNA.
DR   RefSeq; WP_016214000.1; NZ_KE159567.1.
DR   AlphaFoldDB; S0J3L4; -.
DR   STRING; 1235790.C805_00929; -.
DR   PATRIC; fig|1235790.3.peg.980; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_005015_3_2_9; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000014176; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014176};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          187..307
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          678..763
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          777..833
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   835 AA;  96797 MW;  C37C6448F76187D4 CRC64;
     MIQQKLNNNW QMHGPGEPLR PAAVPGTVYT DLLRRGEMED PFWKDNEIRA LSLMEKDYEY
     VTCFDAEKEL LASSRILLRF DGLDTIADIY LNGTQVGAAY NMHRIWEYDV THILKETGNE
     LKVLLHSPLK FIRDAFAECR TLGSEDAMDG FVHIRKAHCM FGWDWGAHLP DAGIFREVTL
     LGITGARLDS VYIRQEHTDG EVSLQFQVEA EREQAVSAHG CAVEKISVKN SGGDENPGSP
     GVAYTVELTT PEGETRTYFD SPAEIHITSP SLWWPNGYGE QPLYQVKVTL YAEGTAVDVW
     ERKIGLRTLT VKTEKDEWGV GFAHEINDIT IFAMGADYIP EDHLLGRVTP DTTRKLLEQC
     VAANYNAVRV WGGGYYPEDW FYDICDELGL IVWQDFMFAC AVYELTPEFK ENIRQEFVDN
     VKRLRHHPSL GLWCGNNEME MFVEEGHHWV TKKTEVRDYI LMYEQLIPEV LKIHDPQTFY
     WPASPSSGGA FDEPNSPDRG DVHYWSVWHG NRPFSEYRKY FFRYASEFGF QSLPARKTLE
     TITDDPRDMN LFSYVMEKHQ RQYGANGKIM NYLQQTYLYP SDFNTLIYAS QLLQADAIRY
     GVEHFRRNRG RCMGAIVWQL NDCWPVISWS SIDYCGRWKA LHYMEKRFFA PLMISCQEEG
     MMTKEADMNR EHFVFEKSIR LNVANETRAD QQVEVFWEVR NAAAEVLRRG EIRQVHVPAL
     TSVWLEKVML PETDIFSEYV SFGMRQNGKV ISEGTVIFSY PKYFRYENPR LSFRLEEDEI
     IISADAYAKS VEIRNEQEDF ILSDNYFDMN AGEKRVKILS GEPQGIRLRS VYDIR
//
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