ID A0A147HXY5_9SPHN Unreviewed; 861 AA.
AC A0A147HXY5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=NS334_13780 {ECO:0000313|EMBL:KTT69755.1};
OS Sphingomonas endophytica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=869719 {ECO:0000313|EMBL:KTT69755.1, ECO:0000313|Proteomes:UP000074310};
RN [1] {ECO:0000313|EMBL:KTT69755.1, ECO:0000313|Proteomes:UP000074310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS334 {ECO:0000313|EMBL:KTT69755.1,
RC ECO:0000313|Proteomes:UP000074310};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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 -!- 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:KTT69755.1}.
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; LDTB01000062; KTT69755.1; -; Genomic_DNA.
DR RefSeq; WP_058756527.1; NZ_LDTB01000062.1.
DR AlphaFoldDB; A0A147HXY5; -.
DR PATRIC; fig|869719.3.peg.2829; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000074310; Unassembled WGS sequence.
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 Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..861
FT /note="Beta-mannosidase B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007547975"
FT DOMAIN 228..335
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 697..782
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 787..857
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 861 AA; 94293 MW; 6420011D17C8A848 CRC64;
MRWLAVPLLL ASTAAVAAPK TVTTLDTDWQ VRIDPKDAEA AKAHPRAAKW FRATVPGSVQ
QALIATKQVP DPFKGTNEAA IQWAGLTGWQ YQRMLRLTPE QMARDHLDLV FDALDTFATV
SVNGQSLLSA DNAHRQWRVD AKPFLKAGDN TITLTFASPI KTMQTKVLAE AHPLPGEYDS
AFGDEPKGKQ TSPYIRKPKY DWSWDWGPRI VNIGPTQPMR LEAWDDARLA QMRVEQVALN
DAEARLDAKF DVVADRTGPA LVRATITGPD GKVVTTEQTI TLAAGDNRVT VPLTIAQPQR
WQPVGYGAQP LYRVAGALVE NGTESDHAKR RIGLRTVELI RGGGAFGFKI NGTPIFAKGA
NLIPFDNFPA RVTPEKMRAL LADAKSVNMN MIRVWGGGYY LPDAFFDAAD ELGLMIWSDF
MFGGAVTPPD AAFRENVRIE AEQQVARVSG HPSIVLWAGG NEVLSGWENW SDRKAFKKAV
GADEQERIGA GMAILFDGVL RQAVRDFDPA VPYWPGSPST DYDGPVDTDA AGDRHFWDVW
SGSKPVANYL NSCPRFMSEY GFQAMPDLAT IKDFAGTLNV APTDPVMKAH QKFLAGEGND
RLLFYIRERL GEPKGLADYV YLTQVNQAQA IELAALHHRA CRPVTMGSLY WQLNDTWPAI
SWSSIDYDGR WKLLQYAARR FFADQVIVTE HKEAATRVAL VSDATTPIAA RWRVRGFAMD
GRVLGERGGD VTLAPLAATE VASVPDAALF GAAAAADSYG VAELYAGDTL LHRRILERAL
PKDMHWPDPG LSARWDGRTV TITATALARA VMLDFGAVSA QPSDDGFDLL PGESRTIRVE
SAATPAQLTR ALTLRSLGGR T
//