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Database: UniProt
Entry: Q5H1Y7_XANOR
LinkDB: Q5H1Y7_XANOR
Original site: Q5H1Y7_XANOR 
ID   Q5H1Y7_XANOR            Unreviewed;       893 AA.
AC   Q5H1Y7;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
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   Name=LacZ {ECO:0000313|EMBL:AAW75034.1};
GN   OrderedLocusNames=XOO1780 {ECO:0000313|EMBL:AAW75034.1};
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW75034.1, ECO:0000313|Proteomes:UP000006735};
RN   [1] {ECO:0000313|EMBL:AAW75034.1, ECO:0000313|Proteomes:UP000006735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735};
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C.,
RA   Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O.,
RA   Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW75034.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5H1Y7; -.
DR   STRING; 291331.XOO1780; -.
DR   KEGG; xoo:XOO1780; -.
DR   PATRIC; fig|291331.8.peg.1980; -.
DR   HOGENOM; CLU_005015_3_2_6; -.
DR   Proteomes; UP000006735; 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; 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; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006735};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..893
FT                   /note="Beta-mannosidase B"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004257448"
FT   DOMAIN          237..346
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          712..799
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          803..880
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
SQ   SEQUENCE   893 AA;  100091 MW;  3E3FC8EC60B3832C CRC64;
     MPLFRPRSVP AAARLGLALA FAISQAWAAP PSAVTLDAGW QVRLVPGQEQ AKTYPKAAAW
     LPAQVPGAVQ TDLIAAKIVP DPFYRDNEGR IQWAGLSDWQ YQTHFNVDAA TLKREHVELV
     FDGLDTCAEV TLNGKQLLSA DNMFRQWRVD AKSLLKRGDN VLEVKLYSPI KKIQPWLAKQ
     PYALPGAYDS AFGDEPEARH SSTYVRKAPY NFGWDWGPRM VNAGIWKDVR VEAWDAVRVD
     GLHIAQQRVD AESAQLQAQL ELQAGRSGPV QVTLDVLGPD GQNVGQFTQD AVVDPGQNRI
     ALAVRIAKPK RWFPAGYGAQ DRYTFVASVR DADGDSQQIK RVTGLRSVEL RREKDTFGKS
     MEIVINGIPI FAKGANLIPL DAFPARVTHD RMRSTLQDAR DANMNMLRMW GGGHYQDDYF
     YDVADALGIM IWQDFMFGGA VPPYDVEFRE NTRQEAIEQV KRLRDHPSIV LWCGNNEVQT
     GWENWGDRVK FKQSVDPEER SRIERGMTTL FGTVFREVVA TYDSDVPYWA TSPGTDFDGA
     ADQANDGDMH YWKVWGGPAL PVTEYLNVTP RFMSEYGLQS FPDMRTVRAF AEPGDLDPES
     PVMRVHQKFD KGNGNKRLML YIRREFGEPK DFESFVYLSQ LMQAEGIHIA ASHLRASRPQ
     SMGSLYWQLN DVWPGASWSS VDYYGRWKAL HYHARRFYAP EMIAALRNDK GQTEVSLVSD
     RTTPLAARWR MRVMRMDGKV LSKREDNASV KPLSSLQVGN FSDKQLLGSA DPKHTYAVFE
     LFDGNTLLSR EMVFFAPAKQ LALPTAKIDS QWRTDGDGYA LTLTSNTLAR DVWLSFGDVD
     ATLSDNAFDL LPGEPLTVHV SSKVALTQLQ SALKVRDLAA TLAGAPPEPA EAK
//
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