ID F5YNT8_TREPZ Unreviewed; 834 AA.
AC F5YNT8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069};
DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
DE AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614};
GN OrderedLocusNames=TREPR_1604 {ECO:0000313|EMBL:AEF85330.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF85330.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF85330.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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 -!- 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; CP001843; AEF85330.1; -; Genomic_DNA.
DR RefSeq; WP_015708517.1; NC_015578.1.
DR AlphaFoldDB; F5YNT8; -.
DR STRING; 545694.TREPR_1604; -.
DR KEGG; tpi:TREPR_1604; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_3_2_12; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000009223; Chromosome.
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; 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 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; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 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:UP000009223};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 189..303
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 658..746
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 751..833
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 834 AA; 95861 MW; 4EB1BBA525873BCF CRC64;
MQKYLLDGEW HLREAGTDKE LSVMIPGSVL EAYTKAGLLP DPYYGENEKN ITSLFEKEFE
YRRSFTVAEE LLAEDTVDLV CLGLDTLGDI ILNGQKIASV NNMHRAWRFG VKSLLKKGEN
EIMIRFHSPN AFIRQAFENG NITYVNLGNM AGSGYLRKAH SQFGWDWGPQ LPDVGIWRSI
FLEASGTARI GDVYITQKHE KGRVDLRLKV RIDTPDRRHF WAEDRRLCGR IRISPPSGSL
IEQQVDLDLD ENTFSITIEN PQLWWPNGLG AHPLYGVELE LLSPGSEDPG SPLDIYRCKI
GLRTMTISTE ADQWGREFAL MVNGLKVFSM GADYIPEDSI IPRVNADRTR KLLEDCVKAN
FNTIRVWGGG YYPDDFFYDL CDELGLVVWQ DLMFACNIYV FTEDFTANVA EEVRQNIRRI
RHHASLGLWC GNNEMEVAWV DWETVRDHPK AVKADYIKLF EVLLPQLARE TDPNTFYWLA
SPSSGGSFDE PNADDRGDVH YWEVWHGLKS FAEYRKHYFR YCSEFGFEAL PELDTIASFS
APEDHNLFSP VMEAHQKCPS GNGKILYYIS ETYRYPKDFA SLVYISQILQ MESIQYGVEH
WRRYRGRCMG AIYWQLNDCW PVISWASIDY YGRWKALHYG ARRFFAPLMV SIFNEVKNIR
LFTHNETPEA VNGLVRLTLR DRDFRALASD EVQVGIPALS AAEVFARDYA ELVNTAELER
SVFVEAELLI DRRVVSRQTA FFAAPKAFSF KRPRYTLDLI ETGDAFVIRL KADTFCRFVQ
LKISGEDVVF QDNYFDIVNS EGREILVLKS DLKDSYTAET LKGKVEILSV GDTY
//
