ID G4RE40_PELHB Unreviewed; 825 AA.
AC G4RE40;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN OrderedLocusNames=KKY_795 {ECO:0000313|EMBL:AEQ50834.1};
OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS B2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Devosiaceae; Pelagibacterium.
OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ50834.1, ECO:0000313|Proteomes:UP000008850};
RN [1] {ECO:0000313|EMBL:AEQ50834.1, ECO:0000313|Proteomes:UP000008850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC {ECO:0000313|Proteomes:UP000008850};
RX PubMed=22156395; DOI=10.1128/JB.06343-11;
RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL J. Bacteriol. 194:197-198(2012).
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; CP003075; AEQ50834.1; -; Genomic_DNA.
DR RefSeq; WP_014129983.1; NC_016078.1.
DR AlphaFoldDB; G4RE40; -.
DR STRING; 1082931.KKY_795; -.
DR KEGG; phl:KKY_795; -.
DR PATRIC; fig|1082931.4.peg.789; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_3_2_5; -.
DR Proteomes; UP000008850; 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:UP000008850}.
FT DOMAIN 207..300
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 743..823
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 825 AA; 93024 MW; FBB7C2EF85275709 CRC64;
MAEAHAASQK VIDYRALDLG GRFALSAPER GWSGEIELPG DVHNALLQAG EIPDPYFGQN
EDIVAWVYKT PWTVERRFDV PAAMAQGYLT LTLSEVDCIA TVFLNGEEIA QTQNQFIRYD
LDVTGKIGAG ENTLTIAFAA VPEIAQSRAD AHPFAIPYAA MNQKVAHLNF VRKTACHAGW
DWGICLMPIG VYGRMELRRS ALARTESVQV EQHHEDGKVN LVLKTRVHAF DSGVVSLTHT
IDGQTVGGDV TVEKGENLIE HTVIIDRPNL WWPAGQGAQP LYDLITDLDG ETTARKIGLR
QLEWIVEADE IDHSFKCRIN GRDITMMGAN WIPADAIPSR ITPEVVEDLL QSARAANYNM
VRVWGGGQYE PDWFYDLCDE MGLLIWHDFM FSCMPYPSDR AFLADVQIEI TQQVRRLSYH
ASIALWCGDN EVIGSLNWYP ETKANRDRHL ANYDRLSKLL AETVEDEDPQ RRFWPSSPSL
GYMDFADGWH IDTRGDMHFW DVWHSAKPFE HYRTVQPRFA SEFGFQSFTS MNVIESFTDP
KDRNPSSPVM ETHQRNDGGN ARILETMCRY FRFPKGFEEM VFLSQIQQGL AIKTAIEFWR
STKPRCMGTL YWQINDIWPV ASWSSLDYGG QWKPLHYLAK RFFAPINIVA VPEGDDIVIK
GMNDGPTPTD ITLNVFSVDM EGNAKPLHGL DVSLGLESAS ELVRVAREAV SAGQFLMLEW
RDRNGVMIGS NDFFPRAHKY YDLPQARIEA RWTRGPSGPE LTLQSDACAF FVTAQVEPAG
YFSDNCFTLL PGRPVTLSFS PRRGAAPGLD DLQNSLRISH LAETY
//