ID   A0A0N7I476_9MICO        Unreviewed;       686 AA.
AC   A0A0N7I476;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN   ORFNames=AOA12_16115 {ECO:0000313|EMBL:ALJ21343.1};
OS   Microbacterium sp. No. 7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ21343.1, ECO:0000313|Proteomes:UP000059097};
RN   [1] {ECO:0000313|EMBL:ALJ21343.1, ECO:0000313|Proteomes:UP000059097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 7 {ECO:0000313|EMBL:ALJ21343.1,
RC   ECO:0000313|Proteomes:UP000059097};
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete genome sequence of a polypropylene glycol-degrading strain
RT   Microbacterium sp. No. 7.";
RL   Submitted (SEP-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         ECO:0000256|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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; CP012697; ALJ21343.1; -; Genomic_DNA.
DR   RefSeq; WP_054687126.1; NZ_CP012697.1.
DR   AlphaFoldDB; A0A0N7I476; -.
DR   STRING; 1714373.AOA12_16115; -.
DR   KEGG; mio:AOA12_16115; -.
DR   PATRIC; fig|1714373.3.peg.3314; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000059097; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059097}.
FT   DOMAIN          26..396
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          408..608
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        162
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        319
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   686 AA;  75805 MW;  744BF9B1C22AD806 CRC64;
     MTARAAAHRW VRPGALGAGG LRYGADYNPE QWPRDVWHED MRLMREAGVN IVSLGIFSWA
     LLEPRPGEWD FGWLDEVMDL LHDNGIDVDL ATATASPPPW LTRLHPEVLP VTADETVLYP
     GGRQHWRPTS PVFRRYALRL VRALAERYRD HPALVAWHIS NELGCHNAFD YSDDAAAAFR
     VWLRGRYGTL DALNDAWGTA FWSQHYGAWD EILPPRIAAA QRNPGRQLDF ERFSSDALRE
     HLRAEAAVLA EVTPDVPRTT NFMVCQNIRD IDYATWAGDV DFVSNDHYLR PGELGRDDLS
     FWANLTGNLA EGHPWFLMEH ATSAVNWREV NPPKRAGELR RDALTHVGHG ADAVCYFQWR
     QSRAGGERYH SAMVPHAGAD SRVFRDVVAL GAELRALAPV AGSHRERARV ALLFDYESWW
     VSGRDSHPSD ALRYDAETLT WYRALLDRGV RVDVLPVHAA FEGYEVVIAP MLHVVPDGLR
     RRLEEVVLDG RHVLATYFSG VVDEHDRVWL GGYPGGLRDL LGVTVEEFVP LLPGTRVRLS
     SGAVATTWTE RITRVGADVE VIDTYADGDL AGGPAVTRRR VGGGSATYVS ADVARAGAVD
     LLRAWAAEVD ALRGEPLAAD GRLETIVRAK GGTRFVFLAN RTDEAVDVPV TGERVGAGGA
     GAERAGTEPV WRIGPGEVAI VAQPGS
//