ID W4D871_9BACL Unreviewed; 881 AA.
AC W4D871;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN ORFNames=C173_21717 {ECO:0000313|EMBL:ETT63761.1};
OS Paenibacillus sp. FSL R7-277.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT63761.1, ECO:0000313|Proteomes:UP000019051};
RN [1] {ECO:0000313|EMBL:ETT63761.1, ECO:0000313|Proteomes:UP000019051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT63761.1,
RC ECO:0000313|Proteomes:UP000019051};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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:ETT63761.1}.
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DR EMBL; ASPX01000079; ETT63761.1; -; Genomic_DNA.
DR RefSeq; WP_036728417.1; NZ_ASPX01000079.1.
DR AlphaFoldDB; W4D871; -.
DR PATRIC; fig|1227352.4.peg.4342; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000019051; Unassembled WGS sequence.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
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; PF02836; Glyco_hydro_2_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
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:ETT63761.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 198..311
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 330..542
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 881 AA; 99591 MW; 30F4B996D92073AB CRC64;
MREILLNELN WEVKGYWPWV PLKGTSMELG QELMGVTDWM PATVPGGVHY DLYRQGWIAN
PYEDLNSLSC EWVENRWWVY RMTLKRPELK GARVELVFLG LDYEAAVYAD HILLGEHKGM
FDPAVYDVTE LLSVREKLEI SVLLKQAPDE MGQIGKTSAT FTQKSRFNYK WDFSTRLVNV
GIWDDVLLRI HEDYSWGEMS ITTDAEVEEG STTQVTGRIE IQAAVPSTAG AEPARTLEAN
ITCSDPGGNP LLVQTLPVCA GAMLKTALDI PEPELWYPNG YGAQPLYCLE LKLLDEDGKE
LDTRVIRTGI RKLDYIRNVD SPDNALPYTV VINGRRIYMK GVNMTPLDHL YGNVTAEQYQ
LMVRLMKAAH VNLVRVWGGG IIEKQVFYDL CDANGIMVWQ EFIQSSSGID NIPSKQPEFL
ELLHQSARSA LKAKRNHVAM TIWSGGNELM SEPNKPSDLS DSNLAMLKEL VEQYDPQRLF
LPTSASGPVE YISETKGQGH DVHGHWKYMG NPYHYELYGS NDNLLHSEFG VDGLSSLKSL
EKFLGAAHRQ PVSMENSAVW RHHGEWWDTL SRDEEIFGSL TDLAQFSACS QWIQAEGIRF
VLEANRRRKF RNSGSIVWQL NEPWPNVSCT NVVDYYGEPK MAYHWMKQAF RPLHVSLDYR
SLLLTPGTGF QGDVYVHGWE GESCEADAEV LDSAGRSLHR QHFITQGDRD RAVCAGTLKF
TVPELEDQLY FVRLSFMNRE EEPQQNVYVF STAREHLYAP ALALTGGKLQ VCQENKWLPA
VTGEPSLQAC FMVANTGSEA LLHVHAEEKG NRYWMEADEQ FLTLFPGEAK MVTVTCTPRQ
AGGFLAGENH SISGDLPVIQ FKSFLAVQGT SKPDRGQENR E
//
