ID D2S257_HALTV Unreviewed; 845 AA.
AC D2S257;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=Htur_4671 {ECO:0000313|EMBL:ADB63454.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG Plasmid pHTUR02 {ECO:0000313|EMBL:ADB63454.1,
OG ECO:0000313|Proteomes:UP000001903}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63454.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB63454.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RC PLASMID=pHTUR02 {ECO:0000313|EMBL:ADB63454.1,
RC ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001862; ADB63454.1; -; Genomic_DNA.
DR RefSeq; WP_012945698.1; NC_013745.1.
DR AlphaFoldDB; D2S257; -.
DR SMR; D2S257; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GeneID; 8745272; -.
DR KEGG; htu:Htur_4671; -.
DR HOGENOM; CLU_005015_3_2_2; -.
DR OrthoDB; 38162at2157; -.
DR Proteomes; UP000001903; Plasmid pHTUR02.
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; 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 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; PF02837; Glyco_hydro_2_N; 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; 3.
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, ECO:0000313|EMBL:ADB63454.1};
KW Plasmid {ECO:0000313|EMBL:ADB63454.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 57..126
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 193..283
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 676..764
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 767..840
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 845 AA; 95534 MW; F6976BBA33FF2ABD CRC64;
MRIESLNGSW KLRQSDTDRW LDASVPGGVY TDLLNAGEIP DPYDDDNELD LQWVGTSDWV
YRHTVTLDDD FLDEERVRLR CAGLDTIATV RINGTVVGEA ANMHRKYEFD VGDALTPGEN
QVEITFHSPV EYSVRHSENH GYQVPTLRYP VDQPGRNFIR KAQCHYGWDW GPCLPTSGIW
RDIDLLAYSE PRIEYTKTVQ DHDGNSVSLD VTVGLDAPAD GDVLLAAEVA NTATHKVVDV
VEGHNEVTIT LDVSDPDLWW PNGYGDQPLY DLIIAVDTKP ESVADDTDAV TADGGVTTAA
SSLLPDPAHE TSTRIGFREL ELVREPDGEG DGESFTFEVN GVSVFAKGAN WIPADALYGR
ITRDRYESLL DSAIEANMNM IRVWGGGYYE RDGFYEACDE RGLLVWQDFM FACALYPSDD
DYLASVEEEV RYQVRRLADH PSIALWCGNN EVEMGLESWF DDADELEQLK EDYETLFYDV
IGDTVAEEDE TRTYWPGSPS SGTGRQDPYP ANKGDIHYWD VWHDGADFEE YETVEPRFVS
EFGYQSFPSV DALSSVLPDN ELNPTAPLME HHQRHEEGNR TILQRMAALF RIPFSFADFV
YLSQVQQGLA MKVAIEHWRR LKPDCMGTLY WQLNDLWPCA SWSSIEYGGD WKALQHVSRR
IYAPVLLSTT MTDDGDEVEI WLTNDERDHL KGNVAVEAYT FDGERIDGTD ERVSVAALDS
ARVATVNADR LLGDIPREEA FLRVTFDGSD ETYPAFTFFE EYKHLELPEP NFDVAVDRNE
VTIKADAAAL FVELNVPLDG QFSDNYFHLT PGEEQRVAFN AADPPDDLER RLTEELSLNH
LRATY
//
