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Database: UniProt
Entry: A0A1X7GQU0_9ACTN
LinkDB: A0A1X7GQU0_9ACTN
Original site: A0A1X7GQU0_9ACTN 
ID   A0A1X7GQU0_9ACTN        Unreviewed;       791 AA.
AC   A0A1X7GQU0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Beta-galactosidase/beta-glucuronidase {ECO:0000313|EMBL:SMF73355.1};
GN   ORFNames=SAMN02745830_05649 {ECO:0000313|EMBL:SMF73355.1};
OS   Streptomyces sp. Amel2xC10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF73355.1, ECO:0000313|Proteomes:UP000192930};
RN   [1] {ECO:0000313|EMBL:SMF73355.1, ECO:0000313|Proteomes:UP000192930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF73355.1,
RC   ECO:0000313|Proteomes:UP000192930};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FWZW01000014; SMF73355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7GQU0; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000192930; Unassembled WGS sequence.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:InterPro.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Gene3D; 2.80.10.50; -; 1.
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; 1.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 1.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF110221; AbfB domain; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
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:UP000192930};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           45..791
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012597965"
FT   DOMAIN          88..210
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          263..343
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          386..497
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          646..785
FT                   /note="Alpha-L-arabinofuranosidase B arabinose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF05270"
FT   REGION          46..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   791 AA;  86757 MW;  2282165239CB1DF1 CRC64;
     MRQAPAGRRQ FGWLRRRARW TVTALVALVL AAATALTATG PATAAGSAAQ AWTPKPSPMT
     TPWTNQVPTD TPLAEYPRPQ LTRPDWANLN GIWDFAVTSA DAGRPASFTE QIRVPFAAES
     ALSGIQRRIT QNDKLWYKRT FTVPSNWNGR RVQLHFGASD WRTTVWVNDR QAGAVHSGGY
     DAFSYDITDL LVGGGTNTVV VSVWDPTETG GQAVGKQRIR DVAPHAGGGI FYTAASGIWQ
     TVWLEPTAPA YIGRLDLVPD PANNRLKVTV RGTGTNGHQA RVTVSTGGTT VGTATGPVGT
     EFTVPVPDPR LWTPDDPFLY DVRADLLSGA NTVDSVGSYT GMRTVGLARV DGLLRPVLNG
     RFVFQTGTLD QGYWPDGIYT APTDAALRHD LQKHKDLGFN MVRKHIKVEP QRWFYWADRL
     GLLVWQDMPS MDLRTPDSAA RTQWEAEYDR VIDQHRSSPS LVMWVDQNEG WGQYDQARIA
     TKVKAYDPSR LVNNMSGVNC CGSVDGGNGD VVDDHVYVGP GTTVPSATRA AVLGEFGGLG
     YKVAGHEWYP GGGFSYEDQP DVAHLNNRFV GLLDAIREVR MPRGLSASVY TEITDVENEA
     NGLLTYDRQV VKVDEARVRA ANRALIDASR AAPAPVTLPV DQYRSLRVTT PGHTDRYLRH
     RDGAAYTDVV NGGSTALLKN DATWKIVPGL ANSSCYSLES RNYPGQYLRH RDFRVYKEAG
     STGLFRADAT FCPVRGANGG VRLSAYNFPE QYLRHYNAEL WLATPGGTHT WDNPALFTED
     TTWSVDAAWA P
//
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