ID A0A0A2DQ39_9PORP Unreviewed; 875 AA.
AC A0A0A2DQ39;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN ORFNames=JT26_09485 {ECO:0000313|EMBL:KGN67447.1};
OS Porphyromonas sp. COT-108 OH1349.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1537504 {ECO:0000313|EMBL:KGN67447.1, ECO:0000313|Proteomes:UP000030126};
RN [1] {ECO:0000313|EMBL:KGN67447.1, ECO:0000313|Proteomes:UP000030126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-108 OH1349 {ECO:0000313|Proteomes:UP000030126};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-108_OH1349 Genome sequencing.";
RL Submitted (AUG-2014) 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}.
CC -!- SIMILARITY: Belongs to the peptidase C25 family.
CC {ECO:0000256|ARBA:ARBA00006067}.
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:KGN67447.1}.
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DR EMBL; JRAH01000034; KGN67447.1; -; Genomic_DNA.
DR RefSeq; WP_036848935.1; NZ_JRAH01000034.1.
DR AlphaFoldDB; A0A0A2DQ39; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000030126; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR006102; Glyco_hydro_2_Ig-like.
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; PF00703; Glyco_hydro_2; 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; 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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000030126};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..875
FT /note="beta-mannosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001997927"
FT DOMAIN 90..158
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 239..335
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 794..860
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 875 AA; 101549 MW; 259FF57364C50402 CRC64;
MNKNRSILLL LFLTLLIPSR LSTYADASNR VGIKSEVLRN WRYKSLKDTL WSSCVVPSVV
QENLIKEKRL SLPYYRDNEK KVQWVSDQDW VYATSFDISE IDRTSGTRQM LEFDGIDTFG
EVYLNGEHLG STKNMFLAYS YDVTGKLVKG ENHLVVHLKS PIGTVHSQYL SNGFNYPADN
DHFPIRYSPF TRKAPYHYGW DWGMRMVTMG IWKEVRLSTY HTARIAFVDV ESKIEWSGEN
SAKQASVVVN VECDSFDKEV YFAQAELTSK QNGKKWSADM DKSGLQKKTF RFLIQDPELW
WPREWGKANL YTLTIRLLDK DKKEIDRNIS EIGIREIKLI NKPDDKGTSF YFEVNRRPIF
AKGANYIPGN LMLTTRTDEY FKSLFDDVEF ANMNMIRVWG GGAYEDDRFY TEANRRGLLV
WQDFMFGCTA YPADSSFLDN VRQEAIYQVK RLRNHPCIAF WCGNNEIEEG ILYWGWQKRL
SPQHYQQLKD SYAPLFHELL PSIIKEYAPR FDYIHGSPMG SNWGQPQTFT NGDIHYWGLW
YGKQPFEVFD KYPMRFVSEY GFQSFPSMKT ISTFALPEDY GLETEVMKVH QKASTGNGLI
KEYMEREYVV PEKFEDFVYV GQVLHGRGMA KSIRSMRRER PTCMGSLYWQ LNDAWPAVSW
SSVDFFQNYK GMHYTTREAY APVAVMTKDI GKDSLAIFVA NDKLNALPGG SLRLETKTVQ
GKKLYTKTIS LPVIAANSVT QVGLFSKRDI AMAENITERV LSISVSTKED NARLLWYAVA
TKDMDLPDQV LKYKVIKQTD GEAVVRFQSE RLVKDLFIET PWHATRFSDN FFDLFPGEQR
DIIIRHAEIS KKTPLKLELK TMNEIHNKYK IIGTI
//