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Database: UniProt
Entry: A0A017HJV9_9RHOB
LinkDB: A0A017HJV9_9RHOB
Original site: A0A017HJV9_9RHOB 
ID   A0A017HJV9_9RHOB        Unreviewed;       814 AA.
AC   A0A017HJV9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=beta-mannosidase {ECO:0000256|ARBA:ARBA00012754};
DE            EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754};
GN   ORFNames=Rumeso_03896 {ECO:0000313|EMBL:EYD74600.1};
OS   Rubellimicrobium mesophilum DSM 19309.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD74600.1, ECO:0000313|Proteomes:UP000019666};
RN   [1] {ECO:0000313|EMBL:EYD74600.1, ECO:0000313|Proteomes:UP000019666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD74600.1,
RC   ECO:0000313|Proteomes:UP000019666};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:EYD74600.1}.
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DR   EMBL; AOSK01000111; EYD74600.1; -; Genomic_DNA.
DR   RefSeq; WP_037282352.1; NZ_KK088604.1.
DR   AlphaFoldDB; A0A017HJV9; -.
DR   STRING; 442562.Rumeso_03896; -.
DR   PATRIC; fig|442562.3.peg.3843; -.
DR   HOGENOM; CLU_005015_3_2_5; -.
DR   Proteomes; UP000019666; Unassembled WGS sequence.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
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   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   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, ECO:0000313|EMBL:EYD74600.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EYD74600.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019666}.
FT   DOMAIN          214..282
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          729..801
FT                   /note="Beta-mannosidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF17753"
FT   REGION          779..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  90745 MW;  5C3204F1ABE12F8F CRC64;
     MNTPISAIQD LAGPWSLTDA TGEHSCLMRV PGDGITALHE AHQIPEPYWG RNEVRLRWIA
     ERDWTIRRQF DLADPEVVLV IDGLDTVATV RVNGTEVLRA ANAFRTWRVD LSGVARRGAN
     TVEIAFHSAP KEAARLAAEQ PFPVPYIHQN NPIPHGNMLR KVACDWGWDW NIALCPFGIT
     GGIWLEEADA PRIERLAVAQ EHEDGRVALT VTAWAENAEG APFRITFAGQ AAEGVLEDGG
     VSVIFDVENP QLWWPAGLGP QTLYDLEVRI GDDVARRRIG LRKMELVSEP DAAGRSFGIR
     VNGRPVFARG ANWIPTDALS GRITEEATRD LLQSAAGAHM NMIRVWGGGR YEPDSFYDAC
     DELGLMVWQD FMFSCNLYSS TPGFLAEVDA EVRENVARMH HHACLALWCG DNELIGALTW
     FPESRNDRDR YLASYDRLNR TIETALRETD PAANWWPSSP SAGPLDFRDA WHVDGTGDMH
     FWSVWHEGKP FDHYRDVSPR FCSEFGFQSY PSMDVIRTFA GPEDWNIASP VLESHQRNAS
     QDGGPDGNAR IAATMFRYFR WPERFEDFVW LSQVQQGMAI KTAVTHWRSL KPHCQGTLYW
     QLNDTWPVCS WSSLDYGGGW KVLHHMARDF FRPVLVTAVP GPEGIALVGV NDTLAPVEIT
     VTAYATALNG AAREIGRGQG TVGEGAERLL LVAPDALGEQ EVLTFGWEAS DGSRAGDVFA
     PRPWKAYDLP DPQLAHQVTR DGDRWVLSVN ARAMAFFVTA EADLPGRWDR NAIHLGPGRT
     ARLTFTPQSP GREPRFALRD LHSATTGRQD QRTA
//
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