ID A0A0C1FBL2_9FLAO Unreviewed; 654 AA.
AC A0A0C1FBL2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Beta-mannosidase {ECO:0000256|ARBA:ARBA00015707};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Lysosomal beta A mannosidase {ECO:0000256|ARBA:ARBA00032581};
GN ORFNames=OA85_12450 {ECO:0000313|EMBL:KIA85419.1};
OS Flavobacterium sp. AED.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423323 {ECO:0000313|EMBL:KIA85419.1, ECO:0000313|Proteomes:UP000031403};
RN [1] {ECO:0000313|EMBL:KIA85419.1, ECO:0000313|Proteomes:UP000031403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AED {ECO:0000313|EMBL:KIA85419.1,
RC ECO:0000313|Proteomes:UP000031403};
RA Gale A.N., Newman J.D.;
RT "Flavobacterium sp. AED Genome.";
RL Submitted (OCT-2014) 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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:KIA85419.1}.
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DR EMBL; JSYM01000003; KIA85419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1FBL2; -.
DR STRING; 1423323.OA85_12450; -.
DR Proteomes; UP000031403; 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; IPR041625; Beta-mannosidase_Ig.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006104; Glyco_hydro_2_N.
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; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF17753; Ig_mannosidase; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIA85419.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 72..140
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 226..387
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 579..649
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 654 AA; 76543 MW; EB7FDB4E1135C9D1 CRC64;
MCCFTNLFFV ANAQNSSIVL KNGWQFRQEK TAKWNAASVP GEVHTDLLNN KLIPDPFYRD
NEKKLQWIEK KNWEYKTSFQ VNSGTLNKKN VELVFDGLDT YATVYLNEKL ILKADNMFRQ
WRVDVKKIIK SGNNDLVVVF QSAQNVVDSL AKKDLPFIIP DNPRAYVRKA QYHFGWDWGP
KFTTCGIWKA VRLETYDEKT PEKPYVLNRK IELVQQPDSL GKSFYFKIDG KPVYMKGANY
IPSDAFLSRV TKKEYEKVIA MAKDANMNML RVWGGGIYED DFFYDLCDKY GINVWQDFMF
AGTMVPGDKA FFDNVKEEVQ YQVKRLRHHP SIVLWCGNNE SDEAFKNWGW QKTMNMPKQD
SIRLWKDYVR LFQDSIPKWV KEVDNKRPYI SSSPLFGWGK KQSITEGDSH YWGTWWGLED
IEVVKNKTGR FVSEYGMQAM PNYSSIEKFT SPEDRYLFSD VLKAHQKAGK GFTKLNSYLN
RYFIDSTKVK NMKVADYTYL TQCLQYYSLK NIIGIHRSKA PYNMGTVVWQ LNDCWPVASW
SVTDYYNRQP KAAWYAMREA YRDDKTPEID LTRPIDLKLE NPKISWIIKG NEIIIKALKP
AKYVYVEIKG YKGKLSTNYM DLKAGEEMKI SFEGKITKPI ITVTSLYDVI NRYK
//
