ID C9Z272_STRSW Unreviewed; 663 AA.
AC C9Z272;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=SCAB_25581 {ECO:0000313|EMBL:CBG69664.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG69664.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG69664.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG69664.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(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; FN554889; CBG69664.1; -; Genomic_DNA.
DR RefSeq; WP_013000352.1; NC_013929.1.
DR AlphaFoldDB; C9Z272; -.
DR STRING; 680198.SCAB_25581; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR GeneID; 24306008; -.
DR KEGG; scb:SCAB_25581; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_11; -.
DR Proteomes; UP000001444; 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: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};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT DOMAIN 22..388
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 400..601
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 611..662
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 663 AA; 73624 MW; A89D1DE9359F5407 CRC64;
MPGETRPSLA AVTRGRVLFG GDYNPEQWPE EVWHEDVRLM REAGVTTVTL GVFSWAKLEP
RPGAREFGWL DTLMDLLHAS GVGVVLATPT SSPPPWMGRL HPETLPRDEN GQVEWWGSRQ
HFSHSSATYR RYAAAITEDL AARYAGHPAL TLWHINNEYC TYDWGDEAAA AFRDWLRRRY
GTLDALNRAW GTAFWSQSYD GWHEIIPPRR AHYLRSPTHV LDFRRFTSDM LLECYAIERD
IVRRHTPHIP VTTNFMPMWA GQDAWRWAGE EDVVSVDIYP DPRDPLGAQH GALVQDMTRS
QAGGGPWMLM EQAAGPVNWR GVNHPKPRGL NRLWSLQAVA RGADAVCFFQ WRQSRQGAEK
FHSGMVSHAG EQGRTYQEVK RIGAELAAVG PAVAGRPLHA EVAVLFDWHS WWAGDHDGRL
SSEVDLAEVV RSWHRALWES NLTTAFAHPG HDLSAYRMVV VPQLYLLTDA AVENLLAYVR
GGGTLVSGFL TGVADEDDRV RPGGMDARLR DLFGIRTLHE RWPLDAGEEV GCAGPRGVFR
GSLWSEEIEA ADADETFAYK GGELDGHPAL LRRGRAWYVS TLPEPAALRD LLAGVAADAG
VRPVLDGLPD GVEAVRRGDV LFVLNHGRDA VTVEVPGTLH DLLTGAVVTG TLSLGRYGVA
ALR
//
