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Database: UniProt
Entry: Q9X0S2_THEMA
LinkDB: Q9X0S2_THEMA
Original site: Q9X0S2_THEMA 
ID   Q9X0S2_THEMA            Unreviewed;       649 AA.
AC   Q9X0S2; G4FEF1;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 128.
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=TM_1195 {ECO:0000313|EMBL:AAD36270.1};
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36270.1, ECO:0000313|Proteomes:UP000008183};
RN   [1] {ECO:0000313|EMBL:AAD36270.1, ECO:0000313|Proteomes:UP000008183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC   {ECO:0000313|Proteomes:UP000008183};
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., Heidelberg J.,
RA   Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., Smith H.O.,
RA   Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD36270.1; -; Genomic_DNA.
DR   PIR; H72283; H72283.
DR   RefSeq; NP_229000.1; NC_000853.1.
DR   RefSeq; WP_004080133.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X0S2; -.
DR   SMR; Q9X0S2; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   PaxDb; 243274-THEMA_08355; -.
DR   DNASU; 898289; -.
DR   EnsemblBacteria; AAD36270; AAD36270; TM_1195.
DR   KEGG; tma:TM1195; -.
DR   KEGG; tmw:THMA_1221; -.
DR   PATRIC; fig|243274.17.peg.1200; -.
DR   InParanoid; Q9X0S2; -.
DR   OMA; SRRHYCF; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000008183; 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: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:SF2; BETA-GALACTOSIDASE YESZ; 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.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008183};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          5..392
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          401..591
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          599..646
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        141
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        314
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   649 AA;  75477 MW;  4ABEC2D73B8D9380 CRC64;
     MLGVCYYPEH WGTEKVEEDF RRMKELGIEY VRIGEFAWSR IESERGKFNW DWLDKTLELA
     EKMGLKIVLG TPTATPPKWL IDEHPEILPV DKDGRVKNFG SRRHYCFSSP VYREEVKRIV
     TIIVKRYGKH PAVAGWQTDN EYGCHDTVRC YCPRCKKAFQ KWLERKYEGD IKKLNEAWGT
     VFWSQEYRSF DEIELPNLTP ADPNPSHLLD YYRLASDQVV EFNKLQVEII REYSPGRFIT
     HNFMSGFTDF DHYKLSKDLD FATWDNYPLG HTLVFLRMKG ETKNPFDRVG HPDIISFSHD
     LYRGVGRGRF WVMEQQAGPV NWAPYNLWPA KGAVRLWTWQ AFAHGAEVVS YFRWRQAPFA
     QEQMHSGLLA PDSAPYPGYH EVKQVFEELK NIDINEPVES EVALVFDYET AWVFSIQPHG
     EGVNYIDLVF RFYSALRRLG LNVDIVPPGS SLDGYKMIVV PSLAIVKEEV LDTFKKYDGL
     LVLGPRSGSK TETFQIPPEM PPGLLKEIIP VEVRQVESLG DNVETLVWNG KEYPVSIWRE
     DVDPTITEVI ARFKDGFGAI FRKENVFYLA FWPNGDFLVD FFEALSKESG IETKRMPEGV
     RIQRRGEYVF SFNFTSEEVD LEIPTKVQIV LGDQKIPPYG LLIWKENER
//
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