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Database: UniProt
Entry: D1BUF6_XYLCX
LinkDB: D1BUF6_XYLCX
Original site: D1BUF6_XYLCX 
ID   D1BUF6_XYLCX            Unreviewed;       685 AA.
AC   D1BUF6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=Xcel_2151 {ECO:0000313|EMBL:ACZ31169.1};
OS   Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 /
OS   XIL07).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Xylanimonas.
OX   NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ31169.1, ECO:0000313|Proteomes:UP000002255};
RN   [1] {ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Foster B., Clum A., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P.,
RA   Woyke T., Wu D., Gehrich-Schroeter G., Schneider S., Pukall S.R.,
RA   Klenk H.P., Eisen J.A.;
RT   "The complete chromosome of Xylanimonas cellulosilytica DSM 15894.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACZ31169.1, ECO:0000313|Proteomes:UP000002255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07
RC   {ECO:0000313|Proteomes:UP000002255};
RX   PubMed=21304672; DOI=10.4056/sigs.571102;
RA   Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F.,
RA   Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T.,
RA   Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K.,
RA   Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Xylanimonas cellulosilytica type strain
RT   (XIL07).";
RL   Stand. Genomic Sci. 2:1-8(2010).
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; CP001821; ACZ31169.1; -; Genomic_DNA.
DR   RefSeq; WP_012878911.1; NC_013530.1.
DR   AlphaFoldDB; D1BUF6; -.
DR   STRING; 446471.Xcel_2151; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   KEGG; xce:Xcel_2151; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_11; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000002255; 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:0006012; P:galactose 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; IPR013739; Beta_galactosidase_C.
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:SF1; BETA-GALACTOSIDASE GANA; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 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, ECO:0000313|EMBL:ACZ31169.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ACZ31169.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002255}.
FT   DOMAIN          26..393
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          406..618
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          626..683
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        162
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         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         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   685 AA;  74530 MW;  B7BC9742D0BEE111 CRC64;
     MNTPFSPGPD YTGWLPGLDA ICYGGDYNPE QWPEEVWEQD VALMKEAGVN LVSIGIFSWA
     LLEPRDGEFD FAWLDRLIEL LHSHGIRVDL GTPTASPPAW FFRQYPESRV VTKNGTVLGF
     GSRGMAAPSS SDYRRHAVRI ATQLAERYGT HPALALWHVH NEYGAPVGED FSAHAQRAWR
     TWLRDRYVTL DALNAAWGTR FWGQVYGDWQ EVGVPAATPS IANPAQRLDF ARFTDAMLRE
     CFVAERDAIR AHSTVPITTN FMAVACPATD LFAWGREVDI VSNDHYLWAA DPRNYVTLAL
     AADLTRSVAG GKPWMLLEHS TSGVNWQPRN VAKRAGEEQR NAFSHLGRGA DAIMFFQWRA
     SRSGAEKFHS AMIPHAGTNS RIWREVVSLG SVLGQLGELR GSRTQADVAI LWDQESLWAQ
     GLEWRPSEDL QAGERIQTFY DRLWRDGVTV DLAHPSSDLS AYRLVVAPAS YLLTQASAAN
     LTRYVEGGGT LLVSCFSGVV DEFDRVHEGG FMAPLRDALG VQVEELLPLR EGESLSVVGL
     SPSSDDEAAG AVTGTVWAEA LMLGGAEVVG TYASGPAAGD AAITRHTHGA GTGWYLSTVL
     DADALAPLMQ RVYADAGVVP SDLPEDVEVL HRVGEGTEWT VAINHTDADA AVPVGTGAMD
     ALSGAAVDGA VKVPAGEVRV LRRAR
//
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