ID F7XK11_SINMM Unreviewed; 668 AA.
AC F7XK11;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Name=lacZ2 {ECO:0000313|EMBL:AEH83339.1};
GN OrderedLocusNames=SM11_pD0507 {ECO:0000313|EMBL:AEH83339.1};
OS Sinorhizobium meliloti (strain SM11).
OG Plasmid pSmeSM11d {ECO:0000313|EMBL:AEH83339.1,
OG ECO:0000313|Proteomes:UP000009045}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH83339.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH83339.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH83339.1,
RC ECO:0000313|Proteomes:UP000009045};
RC PLASMID=pSmeSM11d {ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(2011).
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; CP001832; AEH83339.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XK11; -.
DR KEGG; smx:SM11_pD0507; -.
DR PATRIC; fig|707241.3.peg.6191; -.
DR HOGENOM; CLU_012430_1_0_5; -.
DR Proteomes; UP000009045; Plasmid pSmeSM11d.
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 Plasmid {ECO:0000313|EMBL:AEH83339.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 24..409
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 418..614
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 621..668
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 668 AA; 74972 MW; 2A182B2EE5C29FE6 CRC64;
MPLTSPNHFN SDARTPGRLE LGVCYYPEQW PRGKWAEDAR RMVELGLSWV RIGEFAWAKI
EPRSGEFHWE WLDEAIDVLG KAGLKVILGT PTAAPPKWLV NRYPEILPVD ATGAVRKFGA
RRHYCFSSRR YRSEAARITE AMARRYGEHI YVHAWQTDNE YGDHDTIYSY SAEAVGAFRL
WLAERYGSID ELNRAWGTSF WSMRYDSFEE IDLPNNLVEE PSPTHGVDFI RFSSDQVKSF
NKAQVDIIRA LSPGRPVTHN FMSQNTDFDH YRVGEDIDIA SWDVYPMGGL LNGRLAAKDK
EHYLRVGDPD QPAFNHDLYR AVGRGRVWVM EQQPGPVNWA AHNQSPADGM VRLWTWLAYA
HGVDMVSYFR WRQAPFAQEQ FHAGLLLPNS EADQGYLEVA EVVAEMKRLP EGEVRGKAQV
AIVLDYESRW ATRVLPQGRS YSASAVALDW YSTVARLGVD VDFIGQHSDI AGYKLILAPD
LVIAEEAFVE RLTRADAKVV FGARSGSKTR DMHIPEGLPP GPLAKLIDIS VSRVESLPEF
HSETVLYGNE AYEAGGWRET VRTSETVIAS FDGEYRNGAP ALVGSDKARY LAVAANGALL
DKVIGDALGW AGLESLPDLG DLRVTRRGNL RFAFNFGRIP AEVPAGASAE FYVGGRTLKP
VDVAIWRE
//
