ID A0A1X7HQ52_9BACL Unreviewed; 852 AA.
AC A0A1X7HQ52;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Beta-mannosidase {ECO:0000256|ARBA:ARBA00015707};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE AltName: Full=Lysosomal beta A mannosidase {ECO:0000256|ARBA:ARBA00032581};
DE AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN ORFNames=SAMN05661091_4828 {ECO:0000313|EMBL:SMF89910.1};
OS Paenibacillus uliginis N3/975.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1313296 {ECO:0000313|EMBL:SMF89910.1, ECO:0000313|Proteomes:UP000192940};
RN [1] {ECO:0000313|EMBL:SMF89910.1, ECO:0000313|Proteomes:UP000192940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N3/975 {ECO:0000313|EMBL:SMF89910.1,
RC ECO:0000313|Proteomes:UP000192940};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose
CC residue from the non-reducing end of all N-linked glycoprotein
CC oligosaccharides. {ECO:0000256|ARBA:ARBA00003150}.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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}.
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DR EMBL; LT840184; SMF89910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7HQ52; -.
DR STRING; 1313296.SAMN05661091_4828; -.
DR Proteomes; UP000192940; Chromosome i.
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; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR041625; Beta-mannosidase_Ig.
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 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; PF02836; Glyco_hydro_2_C; 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; 3.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000192940};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 198..299
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 317..431
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 671..758
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 761..843
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 852 AA; 97212 MW; 59148CC1362E1F06 CRC64;
MKLQLLDNWT FKASDEQEWL PARVPGCVHT DLLRNDKIQD PFYGTNEHDL QWIDKQDWEY
ETSFEVSDEL MAESRLELVF DGLDTYADVY VNGKAVLAAD NMFRSWKIDV KERLVPGSNH
IRIVFRSPIQ EDLPKLEKLG YALPADNDQS EVGGLGEKKV SIFARKAPYH YGWDWGPRFV
TSGIWRECRI EAWSEAVIRD VFIHQEQVTA SVARMKAVVT VEVNDDFDGT LIVTTAGQKW
ERKTQLTGGS NTIELAMEIK EPKLWWCRGL GEPNLYEFRA ELQAEQRTVS HASVRTGLRS
VRLVQEADQA GTSFYIELNG TPVFAKGANH IPNDSFLTEV TAERYRHEIA SAAESNMNML
RVWGGGIYEE DIFYELCDEN GLMVWQDFMF ACSMYPGDEA FLNSVRLEAE ENVTRLRNHP
SIVLWCGNNE IDSAWAHYDE KAGWGWKQQY SNDIREKLWR DYEAIFHEIL PEAVGRCAPG
AEYWPSSPLV SLSRDKNQHA NPETTSGDIH YWGVWHNNEP FDNYNVYVGR FMSEYGFQSF
PEPKTVRTYA GESDMELESK VMLAHQKNGA GNHLIKSYMD QYMHEPKDFT SFLYMSQMQQ
AEAMKTAIEA HRRNKPYCMG TLYWQMNDCW PVASWAGMDY LGRWKALQYV AKRSFRDVCL
AVEQKQEEGI VSVHLISDVS APIEGILRLE LISFEGKELH ALSLPVQVNA QAALIVYQTQ
VDELLSGHNP SSVVLRVELE LEGDVADSKD HYFVTDKHLL LQTPDITVRE VQGNGGTVVI
VESNVFARQV WLSSEQEGIF SDNFFDLIPG KPKKISFSSR HSSETAFIPA SPGTVKVFSM
ADCIHSESLA AR
//
