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Database: UniProt
Entry: A0A0Q4IL85_9SPHN
LinkDB: A0A0Q4IL85_9SPHN
Original site: A0A0Q4IL85_9SPHN 
ID   A0A0Q4IL85_9SPHN        Unreviewed;       997 AA.
AC   A0A0Q4IL85;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=ASE85_10005 {ECO:0000313|EMBL:KQM99062.1};
OS   Sphingobium sp. Leaf26.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1735693 {ECO:0000313|EMBL:KQM99062.1, ECO:0000313|Proteomes:UP000051336};
RN   [1] {ECO:0000313|Proteomes:UP000051336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf26 {ECO:0000313|Proteomes:UP000051336};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001412};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:KQM99062.1}.
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DR   EMBL; LMKV01000028; KQM99062.1; -; Genomic_DNA.
DR   RefSeq; WP_056690422.1; NZ_LMKV01000028.1.
DR   AlphaFoldDB; A0A0Q4IL85; -.
DR   STRING; 1735693.ASE85_10005; -.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000051336; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF13364; BetaGal_ABD2; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..997
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006221761"
FT   DOMAIN          397..572
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
SQ   SEQUENCE   997 AA;  107833 MW;  65A313C9DE0609EC CRC64;
     MRSLIAALLL GSTLAMPAVA QEAKPTANLA APVKTFGRVS YDARSLMVDG KRLVIWGGEF
     HPFRLPSPDL WRDILQKMKA SGYNSVALYF DWGYHSPKQG VYDFSGIRDI DRLLTMAEEE
     GLYVITRAGP YVNAELSRGG FPGWLVNQRA RARTDDPDYL KAADEWLSHI NPIIAKHQIN
     ADPKRRYGVI LHQIENELAL TTPAQRRYMD HLYAKARADG ISVPLFHNDQ GRNGYWAPES
     SKVEKVVHGP NDMYAFDGYP GGTCTVEGKP TRDVAAPDWG FYGPGGAKGG ASASPDTPGF
     LAEFGGGWFD YWGSNGGYEC NAIQRGKRFQ RVFYGTNLAN GIGIQSFYMS YGGTSWGWLP
     APVVFTSYDY GSAISEPRVL RDKAMEMKAL GGLIASVPDL AGMVPAGQPV ISSPNIQIYH
     NKSPETDARF LMVTHKPSNG QTHDAFSFTA DLPDGRYTVP MQLNGFDAKW LVAGVTLNGQ
     RLVYSTSELQ ASLDGVMLLY GRAGEPGETV LRYAGAPKVT VLEGQVSSAF DAAKGDLKLS
     YMHQGRAAVR IEGGEHPPLT LILADEAESA RYWRQGDALV RGPALVRSAT IKGGALTLTG
     DTAGESLLEI WAPAAVRSVM WNRAAVATKR TAIGSLIATQ PLSGPADIAL PALTDWRMAK
     GSPEADPAFD DSAWQAIDRR PYAPTTIRPD GQPNMSMDAY GFHDGDVWYR GRFTGTPDAK
     ALSLFYGAGG AGLVQAWVDG QFIGEAETPT GLPRPITTGT ARFALPAGAQ SGAHVVSVMV
     RNNGHNWDLD SDDFHKEARG LISASLEGGP SGRSFTVPID WKIQGKQGGE DLPDPMRGPA
     NNGGQFGERM GWHLPGFDDR AWGKVSLPAT QMDAGTSWYR TDFALNVPKA QDATIGVRFG
     DASKPRSPVR YRVLIFVNGW NMGQFVAHVG PQRTFPIPEG ILNHRGKNHI ALAVTSDGQP
     GDALESVRLV TLHTVKGGLP VQMVAAPNAP SDLKEIQ
//
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