ID   D1CIF9_THET1            Unreviewed;       669 AA.
AC   D1CIF9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
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=Tter_2642 {ECO:0000313|EMBL:ACZ43530.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Chloroflexota; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ43530.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ43530.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H.,
RA   Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M.,
RA   Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA   Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(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; CP001826; ACZ43530.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1CIF9; -.
DR   STRING; 525904.Tter_2642; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   KEGG; ttr:Tter_2642; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_0; -.
DR   Proteomes; UP000000323; Chromosome 2.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:ACZ43530.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ACZ43530.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          17..383
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          394..599
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          608..666
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        153
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        304
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   669 AA;  76705 MW;  903D6B39CA30DEF9 CRC64;
     MYGPINPKAP FIWHGGDYNP EQWPPEVWVE DVRLMQEAHY NVPTVGVFSW VSLQPDEHTW
     DFEWLDRVLE MLHASGRYFV LATPTAAQPA WMSQRYPDVL RADNTGRRHH HGRRVNYCPN
     SPNYRRFIRE VASRLAQRYG GHPGLLAWHV SNEYGGTCMC EVCAEAFRAW LRRRYGSLEE
     VNRSWWTRFW GHTYTDWSQI TPPYANGENL THGLTIDYKR FQSEAMLECF KIERDAIREH
     SPDVPVTTNL MGTYPLLDYR EWAKEMDVVS WDCYPWPTAD PGDIAFLHDL NRGLKDGRPF
     ILMEQTPSSQ NWQPVNQLKR PGVLRLWSYL AVAHGAETVM YFQWRRGRGG CEKFHGAVVE
     HHGRTDARVF REVSELGAEL ERLGDATIGA ATPARVAVMF DWNNWWAIDD AVGPVREKRY
     VETVRQHYRA IWRKNVPVDV VFSDSDLSRY DLVIAPMLYM VKPGVAERIE GFVRGGGVFV
     ATQFSGVADE HDLAFEGYPG PLRRVLGIWV EEIDALYEGQ VNHIVMADGT GTYECGRMCD
     IVRTETARVV ATYGEDFYAG TPVVTENRFG EGRAYYIASH PEDRFLDEFY GLLLLEQGVQ
     PVMETPAGVE AALREKDGAR LVFLLNHNPE EVTVRLPEGE AFLELLSGEE LRGEIVMAAY
     DVRILRADA
//