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}.
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; 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
//