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Database: UniProt
Entry: G5IC87_9CLOT
LinkDB: G5IC87_9CLOT
Original site: G5IC87_9CLOT 
ID   G5IC87_9CLOT            Unreviewed;       855 AA.
AC   G5IC87;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN   ORFNames=HMPREF9473_01070 {ECO:0000313|EMBL:EHI61005.1};
OS   Hungatella hathewayi WAL-18680.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI61005.1, ECO:0000313|Proteomes:UP000005384};
RN   [1] {ECO:0000313|EMBL:EHI61005.1, ECO:0000313|Proteomes:UP000005384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI61005.1,
RC   ECO:0000313|Proteomes:UP000005384};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA   Molitoris D.R., Song M., Daigneault M., Allen-Vercoe E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium hathewayi WAL-18680.";
RL   Submitted (AUG-2011) 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   -!- 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:EHI61005.1}.
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DR   EMBL; ADLN01000009; EHI61005.1; -; Genomic_DNA.
DR   RefSeq; WP_006779056.1; NZ_JH379027.1.
DR   AlphaFoldDB; G5IC87; -.
DR   PATRIC; fig|742737.3.peg.1075; -.
DR   HOGENOM; CLU_005015_3_2_9; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000005384; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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   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   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:UP000005384}.
FT   DOMAIN          244..336
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          785..830
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   855 AA;  97636 MW;  6C676A87D2E72D4B CRC64;
     MNLFKMELKD WRVGEYPAGA PDGTTPEVPE EWISASVPGC VQYDLVEQGR LDNPYAGTKG
     AFDAAWVAKS DWLYETVFDR PDGLEKMAHV ILKLWGIDTF SEVWLNGSLL GETVNAYRSY
     EFSILPEMLL ERGNRLQIRV KAHGRMVEDK LEAAECLTCG KETEGLLGKA LIRRYQRSFY
     TNSSLLNVGT GVLGIGINRP VELYGYPGRY LTDVAYTTRE IGDCAEGSIC VSLNPAGEDG
     ADQAEKTAEE KCAVQAENLA GEEVVVKAEI LDGEKTCVWE TEYVAGEETT ETAVRIENPK
     LWWPRGYGEP YLYTLKVSVW ENGVQTDEKI IQIGIRTVRL VQRTPSGKKT FYIEVNGQKI
     FVKGENYIPM DYLKVYGSRE QYDNLFLLTE QQLVNTIRIW GGGAVEDESF FRECDRRGIL
     IWHDLFLHSN VYPDYDPEFV ENYKEEVKGV LKTIRSHPCI CLVCGGNEQQ EGWDEWGWKQ
     DKERFFGETL PRVHTPVLVE ELCPDIPYIY NSPHGGSLCQ SPAEGDSHCW GNYYNSFKDP
     LFVTETCWTT ESYSRPETLE SCMGMDLTEY EGKGWADKWN QFTSLPTFNR RPFSSWFETD
     SLRGYLHALE VEQARADYHA LSQLRFTGPS NHGIIYWSFN KGGPLFQFGC VDYGGRPMMS
     YYVVKRLYQS VAIFPYREFK DVRVLLSNHL TCEAEVCVEA FHMNRAGEVL NQFRAETVCP
     AGETVLALLL EGLYEQVQER TEETVFVRAI MDGVVVSEDL LLFAPYGELQ VDSRPMDARM
     EKTGEREWEL TVHSEGIVQM VEIECDRKMV CEDNYFPMMT GERKTVKMIL LEECGGRQPE
     FLIRKLGEKN SIKLH
//
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