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Database: UniProt
Entry: H8H131_DEIGI
LinkDB: H8H131_DEIGI
Original site: H8H131_DEIGI 
ID   H8H131_DEIGI            Unreviewed;       666 AA.
AC   H8H131;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
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   OrderedLocusNames=DGo_PA0164 {ECO:0000313|EMBL:AFD27050.1};
OS   Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OG   Plasmid P1 {ECO:0000313|EMBL:AFD27050.1,
OG   ECO:0000313|Proteomes:UP000007575}.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD27050.1, ECO:0000313|Proteomes:UP000007575};
RN   [1] {ECO:0000313|EMBL:AFD27050.1, ECO:0000313|Proteomes:UP000007575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC   {ECO:0000313|Proteomes:UP000007575};
RC   PLASMID=Plasmid P1 {ECO:0000313|Proteomes:UP000007575};
RX   PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA   Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA   Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA   Lin M.;
RT   "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT   Deinococcus gobiensis: insights into the extreme environmental
RT   adaptations.";
RL   PLoS ONE 7:E34458-E34458(2012).
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; CP002192; AFD27050.1; -; Genomic_DNA.
DR   RefSeq; WP_014695568.1; NC_017805.1.
DR   AlphaFoldDB; H8H131; -.
DR   KEGG; dgo:DGo_PA0164; -.
DR   PATRIC; fig|745776.4.peg.3200; -.
DR   HOGENOM; CLU_012430_1_0_0; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000007575; Plasmid P1.
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: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   Plasmid {ECO:0000313|EMBL:AFD27050.1}.
FT   DOMAIN          20..407
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          419..617
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        154
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        336
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   666 AA;  73208 MW;  2155BF0A31747F89 CRC64;
     MSSLPPSDSL PFLSLGVCDY PEHVPQPLWA GYARDQKALG LEFVRLAEFA WSRMEPRPGE
     YDWAWLDEAV ETSAAAGLKV VLCTPTAAPP AWLVEAHPEI LPVGRDGQVK SFGSRRHYDF
     SSAVYREHSR RITRAVAERY GRHPAVVGWQ TDNEFGWGDT AQSFSPAVHA AFHAWLERRY
     GTVDALNAAW GNVFWSMDYS GWAQVPLPHH AVSEINPAHA LDFLRFSSGE VAAFQAEQVA
     LLREHSPGRF VTHNYMGFFS AYDHYEVSRG LDFASWDSYP TGTLQAIHEW KLLAPHFALD
     YARTGHPDVT AFNHDLYRGM VTPGAGQATP SFWVMEQQCG QVNWASANPL PAPGAVALWT
     EQAWAHGADA VSYFRWRAAT VGQEVLHSGL LRHSGRPDQG HREVAALRPQ ALPLAPTRAR
     VALLHDYESL WLYNLQPHSE GLNYWAQTFT YYRALRALGV DVDILHPDRD LSGYAVVVAP
     ALTLMTPERA AHLTASAGHS RLVFGPRTAF RTAAGGTPET GQFGDLAGLI GAELSRYDSL
     YAGMTQDVEG EGGARHSAHA WAESYDLAGA EALWHYRGGP LDGEAAVVRH GAVTTVGAHS
     ESLVRGVLRG ALREAGVETA ELPEGVRLTR RGPHTLLQNW TGESVHWQGR TLAPYSSALL
     PQEVMA
//
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