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Database: UniProt
Entry: A0A147HXY5_9SPHN
LinkDB: A0A147HXY5_9SPHN
Original site: A0A147HXY5_9SPHN 
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}.
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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
//
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