ID L0A2F2_DEIPD Unreviewed; 832 AA.
AC L0A2F2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN OrderedLocusNames=Deipe_2112 {ECO:0000313|EMBL:AFZ67604.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ67604.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP003382; AFZ67604.1; -; Genomic_DNA.
DR RefSeq; WP_015235909.1; NC_019793.1.
DR AlphaFoldDB; L0A2F2; -.
DR STRING; 937777.Deipe_2112; -.
DR KEGG; dpd:Deipe_2112; -.
DR PATRIC; fig|937777.3.peg.2118; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_1_1_0; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000010467; Chromosome.
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 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:UP000010467}.
FT DOMAIN 198..301
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 752..809
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 832 AA; 94163 MW; E3C163B82F0109B4 CRC64;
MTHLDLHADW QLKPRNPALP LSDDFASPDG WLSASVPGTV QQDLLTQGRI PDPYYGINEH
DVQWVGEQDW LYRVTFDVHE ATLHEEYVRL YFGGLDTFCT VWLNREEVLR SENMFVPRTL
NVKQHLHAGR NILQLLFESP LRVGRALEAQ HGKRAAWNGD KSRLYVRKAQ YHYGWDWGPV
LLTTGPWKSV ELRAFGNAIE DVHVPGEVTP DLQTAFVPVR VQLTQDDPAQ RLVVELRSPV
GEVLQRAELP ASQTAGTLFE LPRPQLWYPN TLGEQPLYSV QVTLWHGEKV VDACCRRIGL
RRLRVVQEAV HGEPGTSFTF EVNNVPFFAG GANWIPDDLL LNRITPERYR ERLTQAQGAN
MTMIRVWGGG IYEPDVFYDI CDELGLLVWQ DFMFGCGMYP AYEGFLTSVR AEAEAAVRRL
RHHPCLALWC GNNEDYAIAE SVGASGPGGD ESRFDARVIY EDLLPEVCAQ LDPARTYWPG
SPWGGVNSAD PTVGDRHSWE IWHGPMAPYQ KYARYEARFV SEFGLQSAPA LSTLHACTPE
RERFPESRTI THHNKATGPN GEGDGHRRLA VYLADNLRAH RTLDEFVYNT QFVQGEAMRY
AYRDFRARFE GPGKYAVSGA LVWQLNDCWP VTSWAIIDSQ GFEKPAYYTI KRELASLSVG
LRLNEGELEI WLSSARTMAL DAQLDVYVYG LDGTLALHET RDVRVWPGRK TELSARCASG
VPQVYFAELT LNGEVVARAA EFPEPFKFYD FPHPELQVEW VAENALRLTA RKPTKGVWLD
TDCPAHWDDN FLDLRPGESR TVTARALNGQ TVRVRFLNAP EALTVSVAPK PS
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