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Database: UniProt
Entry: A0A0A2DQ39_9PORP
LinkDB: A0A0A2DQ39_9PORP
Original site: A0A0A2DQ39_9PORP 
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
//
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