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Database: UniProt
Entry: A0A160KVN5_9MICO
LinkDB: A0A160KVN5_9MICO
Original site: A0A160KVN5_9MICO 
ID   A0A160KVN5_9MICO        Unreviewed;       701 AA.
AC   A0A160KVN5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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=A6122_2328 {ECO:0000313|EMBL:AND17448.1};
OS   Rathayibacter tritici.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=33888 {ECO:0000313|EMBL:AND17448.1, ECO:0000313|Proteomes:UP000077071};
RN   [1] {ECO:0000313|EMBL:AND17448.1, ECO:0000313|Proteomes:UP000077071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND17448.1,
RC   ECO:0000313|Proteomes:UP000077071};
RA   Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT   "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; CP015515; AND17448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160KVN5; -.
DR   STRING; 33888.A6122_2328; -.
DR   KEGG; rtn:A6122_2328; -.
DR   PATRIC; fig|33888.3.peg.2593; -.
DR   Proteomes; UP000077071; 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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 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:UP000077071}.
FT   DOMAIN          17..395
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          407..614
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        152
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        318
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   701 AA;  78039 MW;  FA3BA8A3BDDB3185 CRC64;
     MMPAAPRFSG VLFGAAYYVE YQPEGVLERD LDLMAEAGFT VIRVGESVWS TWEPREGVFD
     LDWLEPVLDA AHARGISVIL GTPTYAIPPW LQRLHPEIAA ESRTGVRMGW GARQEMDQSH
     PAYRFYADRI ARKVVARYAD HPAIIGYQVD NEPGNHLPHN EHTFQRFVGW LRERYGTVED
     LNREWGLVYW SHRLSDWADL WRPDGNLMPQ YQLEWRRFQS TLANELIAWQ ADLVREYARE
     DQFVTTCIAY SQAQISDDEI VAPLDVVAGN PYYKMQGDLD ATAEVPRERP WWGTGVWALF
     EWGDRAFSSA QTQYLVTETN AQSINGSWTN HPPYPGQIKQ AALALLARGG RMIEYWHWHT
     LHFGIETYWG GVLPHSQQPG RIYREVADLG ATLKALGPAL DEYEPDADVL MLYSTDTKWS
     FEFTPPLARA DGSPDSRAYL TIFDAFYRGL FEAGAQIRVQ HLRQFVASDI TELVRRYPVL
     IAPAVYVADD AMLEHLRAYA EAGGHLVLGI RTGYADELAR ARLAVAPAFL TDAAGVHYDE
     YSNIDAPMMV HAEGDLALEE GAAGTEWVDV LEVDDADVLL RYEPTELEAD AAVTTHAFGA
     GRVSSVGTVP NPALGRSIGR WLVPDTQKSQ WHAGDSVSVS TGTTGHSRVV FLSNWSAAAT
     SVTTPAPARD LVTGATYAAG DSVPLDRRGA AVLEIALDAT E
//
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