ID A0A285KJC7_9ACTN Unreviewed; 641 AA.
AC A0A285KJC7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=SAMN05421748_14238 {ECO:0000313|EMBL:SNY72333.1};
OS Actinoplanes atraurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1036182 {ECO:0000313|EMBL:SNY72333.1, ECO:0000313|Proteomes:UP000219612};
RN [1] {ECO:0000313|EMBL:SNY72333.1, ECO:0000313|Proteomes:UP000219612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6857 {ECO:0000313|EMBL:SNY72333.1,
RC ECO:0000313|Proteomes:UP000219612};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OBDY01000042; SNY72333.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285KJC7; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000219612; 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:UP000219612};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 7..375
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 389..579
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 590..640
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 143
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 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 153
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 641 AA; 70945 MW; 6F7A407AC818C66A CRC64;
MITLGCDYNP EQWPAEVWAE DVALMRTAGV SLVAVNIFGW SDLEPRAGEY DFKQLDRIVE
LLHQNDIKIN LGTATASPPP WLGARHPEIL PMAADGTRRY PGGRQAWCPS SPVFREHALS
LVEQVAQRYG QHPALALWHV SNELGCHNAL CYCDASAERF RAWLADRYET VEGLNAAWGT
SFWSQRYGEW SEVLPPRTAL SLRNPAQMLD FHRFSSDELL GYYEAEAAVL RKHSSVPVTT
NFMVTAHIRN MDYWRWAPRM DVIANDHYLD HRLGHPAAEL SFAADLTRGL AGGKPWMLME
QSTGAVNWQP VNLAKAPGEM LRNTLTHVAR GADAVCFFQW RASAQGSEKF HSALLPHAGT
DTEQWREVLD LSSVLGKLAE VAGTTVRTET AVIFSWEAWW AAEQEGRPST AVNYLDQVHA
VHGGLRDLGV TADVISPDGD LSAYAQVIVP CLYLVTDEQA AAIQKYVERG GRVLVTFFSG
IADRDDRIRP GGYPGAFRDL LGVTVEEFAP LKPGTTVTLD DGSKATLWTE RLRTTSAEVV
ARYTDGPLPG TPAITRNGNA WYVATALDRE SMRTVLSRFT GTPETHDGSV EVVRRGTYVF
VINHGEREIE YAVTGHELLR GEKVAGLVKV PAGAVRVVRE S
//
