ID E8N5L4_ANATU Unreviewed; 666 AA.
AC E8N5L4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=ANT_17020 {ECO:0000313|EMBL:BAJ63728.1};
OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS UNI-1).
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Anaerolinea.
OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ63728.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ63728.1, ECO:0000313|Proteomes:UP000008922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC {ECO:0000313|Proteomes:UP000008922};
RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA Fujita N.;
RT "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL Submitted (DEC-2010) 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; AP012029; BAJ63728.1; -; Genomic_DNA.
DR AlphaFoldDB; E8N5L4; -.
DR STRING; 926569.ANT_17020; -.
DR KEGG; atm:ANT_17020; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_0_0; -.
DR InParanoid; E8N5L4; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000008922; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:BAJ63728.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:BAJ63728.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008922};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 16..377
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 390..595
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 611..663
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 151
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 666 AA; 76929 MW; 7627A1C6FA6D33ED CRC64;
MTTQRSRKVL HIGAAYYPEH WKSEQWLSDI RLMQELGLSV VRMGEFAWSS LEPSKGNFQF
EWLDQAINLL ALHDIRTVLG TPTAAPPAWL VSEHPEILAT NEEGRKVQFG NRCHYCVNST
AFHEATAKLV KAMAEHFGSN PNIIGWQIDN EFNRVCYCEH CQALFQEYLK EKYKSLDELN
RRWTTAYWSQ TYNDWSQIPI PIGPHNPALM LEWKRFVTRS YRKFQRMQID LLRPHLREEV
WITHNFMGWF DGFDHYEMST DLDMASWDWY IGMGHNEPVF SSATHDLTRG FKKKNFWVME
IQPNTVNWAK INNPLYKGEA RTMAWQAIGK GADAVLYWQW RSALNGQEQF HGTLVDQSGQ
PRPFFEEVKQ IAKEFRELSS VFEYTQVESR VAILNDYESR WAISWQKHHR DFDYVALLLS
YYRPLCQLNI PVDIISPDQS LEEYKLVLAP ALTIVDEARI AHLKSFVDNG GHLVLGARTA
VKNRDNAFHP LRPPAFLTHL TGAEVEDFYA LNEEVPLQGN WFTGTARIWA ERMKIIDPDS
TLPVATYGVS NGWLDGQIAM TIHNHGSGLV YYAGAYLDDT AMFAYLKRVA TNAGVQGLFE
APAGVQIYRR VRTYDKKEVF VIVNHTRMEQ IVKLDNNTYD DHISGKRIAG QIRLSPYGVA
VLTKTI
//
