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
//