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Database: UniProt
Entry: A0A0P9EXW1_9BACL
LinkDB: A0A0P9EXW1_9BACL
Original site: A0A0P9EXW1_9BACL 
ID   A0A0P9EXW1_9BACL        Unreviewed;       693 AA.
AC   A0A0P9EXW1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=AN477_09620 {ECO:0000313|EMBL:KPV43967.1};
OS   Alicyclobacillus ferrooxydans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV43967.1, ECO:0000313|Proteomes:UP000050482};
RN   [1] {ECO:0000313|EMBL:KPV43967.1, ECO:0000313|Proteomes:UP000050482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC-34 {ECO:0000313|EMBL:KPV43967.1,
RC   ECO:0000313|Proteomes:UP000050482};
RA   Hemp J.;
RT   "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL   Submitted (SEP-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPV43967.1}.
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DR   EMBL; LJCO01000042; KPV43967.1; -; Genomic_DNA.
DR   RefSeq; WP_054968941.1; NZ_LJCO01000042.1.
DR   AlphaFoldDB; A0A0P9EXW1; -.
DR   STRING; 471514.AN477_09620; -.
DR   PATRIC; fig|471514.4.peg.500; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000050482; Unassembled WGS sequence.
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: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};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050482}.
FT   DOMAIN          15..387
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          401..608
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          637..681
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        310
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         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   693 AA;  79039 MW;  D4D9AA237C49FA29 CRC64;
     MTKTLHAKSL KVGVCYYPEH WSSDMWDSDL EMMRHMGITM VRVGEFAWSI FEPKDGEFSF
     QLFDEFIERA GQFGIGVILG TPTATPPAWL TYKYPEVLNV SLDGIQFQHG LRRHYNYNSP
     VYQQYCRRIV EKMAKHYGEN THVIGWQIDN ELNCEIDVFY SERDHEAFRQ WLTVKYGTLD
     RLNHAWGTVV WSQTYTAWEQ VHLTRPNPSH SVNPHQALDE KRFISNSVMR FVENQTEVIR
     QYAPHQFITT NGIFGHLDTH ELTERYLDFI SYDSYPNFGM LADDESLRDR EWSFNLSVAR
     SVSPNFCVME QQAGPGGWVN RIEQPTPLPG QLRLWAFQSL AHGADAIVFF RWRTAPFGTE
     IYWHGIFDYD NQPNRRVAEI GQTINEVSLL ADKLAGSLVQ ADVALLRDYN NDWDGEVDTW
     HGPYTKKSVK EWFRGLQTSH VPCDVLNLSE TTQLADLRRY KVLVYPHPVV LSERVTELLE
     QFVSAGGILI TGCRAGLKDV NGHCRQVSMP GPLKNLFGVQ VSDFTRIQGA YEVPNLVWNG
     DESSSGCIHA VDFNEVLQPT SEDCTVLATY DRNYYSGTPA LVQNSFGKGT TYYYGSVFTR
     ELAKKLIELT GLVDTENKLV STTEEVELEI RRNPLTGDRY VFLLNYSGQP QAVHLHHGCR
     NALNGELIEG DLVLDGYDVL VCEVPDGGAT ARG
//
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