ID A0A1H6ES87_9ACTN Unreviewed; 663 AA.
AC A0A1H6ES87;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05444920_117151 {ECO:0000313|EMBL:SEH00720.1};
OS Nonomuraea solani.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEH00720.1, ECO:0000313|Proteomes:UP000236732};
RN [1] {ECO:0000313|EMBL:SEH00720.1, ECO:0000313|Proteomes:UP000236732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEH00720.1,
RC ECO:0000313|Proteomes:UP000236732};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNVT01000017; SEH00720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ES87; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000236732; 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: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: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 Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000236732};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 21..386
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 398..600
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 610..660
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 157
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 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 663 AA; 72942 MW; 591AE866429433E4 CRC64;
MTARLGMHTL TEGRGLLFGG DYNPEQWPEE VWAEDAALMR AAGVNLVTVG VFSWGRLEPE
PGVRDFGWLD RVLDLMAGHE IAVDLATPTA SPPPWLGHRW PETLPIDESG HRLWYGARNQ
FCPSSPVYRE RALEIVGALA DRYAGHPALA LWHVGNEYGQ VCHCDESAKA FRAWLTKRYG
DLGTLNDAWG TTFWSQHYSD WAEILPPRLA PYIINPAQRL DWRRFCSDAL LEHFRAERDL
LRERAPGIPV TTNFMGLFKP VDYWSWADEE DVVSNDHYPE PGDPMAPALT ALTHDLMRGL
AKGRPWLLME QSTNAVNWRP HNLPKPPGQF RLESLQALAR GADGLCYFQW RASRFGAERF
HAAMVPHAGA DTRLHAEVRA HGQELRGLAA VAGEPVPARV AMVFDWASWW ALEERGRPSD
RLNATDQLLS YYVPYFERGV SVDVVPPSAD LSAYALVVVP NLFLVGDRDA AALTAYVRGG
GVLVVGPFSG VVDPRAQVRT GRFPAPLREV LGASGEEWMP APDDHPVRCR WSDGTEFEAH
TWTELLAAEG AEVVAEFAED GGPAVTRHRS GEGVAWYVGT MPEPAALSAL TGRVLADAGV
TGELPDLPPG VEAVRRGDVL FLLNHGTTTV EVPIPHTTAE DLLTGSPATG HVTLTPRAVA
AIR
//
