ID A0A1C0ANE1_9ACTN Unreviewed; 673 AA.
AC A0A1C0ANE1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=BCR15_03555 {ECO:0000313|EMBL:OCL34768.1}, TLA_TLA_00094
GN {ECO:0000313|EMBL:VEP38607.1};
OS Tessaracoccus lapidicaptus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1427523 {ECO:0000313|EMBL:OCL34768.1, ECO:0000313|Proteomes:UP000093501};
RN [1] {ECO:0000313|Proteomes:UP000093501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPBSL-7 {ECO:0000313|Proteomes:UP000093501};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OCL34768.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IPBSL-7 {ECO:0000313|EMBL:OCL34768.1};
RA Puente-Sanchez F., Arce-Rodriguez A.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VEP38607.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TLA_E {ECO:0000313|EMBL:VEP38607.1};
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000516347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (JAN-2019) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MBQD01000020; OCL34768.1; -; Genomic_DNA.
DR EMBL; LR214441; VEP38607.1; -; Genomic_DNA.
DR RefSeq; WP_068751450.1; NZ_MBQD01000020.1.
DR AlphaFoldDB; A0A1C0ANE1; -.
DR Proteomes; UP000093501; Unassembled WGS sequence.
DR Proteomes; UP000516347; 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:UP000093501}.
FT DOMAIN 16..384
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 402..607
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 614..669
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 306
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 673 AA; 73769 MW; EBBB12CE383A6B2A CRC64;
MTFETLRHEG VWFGGDYNPE QWPPAVLDED LELMERAGIT TVTVGVFAWS SLEPEPGRFE
FGWLDDALER LTAAGIGVVL ATPTASPPPW FSRLHPEGLP VTADGVRLIH GSRDTYNPAA
PAYREAAARI TRALAERYGS HPALRMWHLH NEYGTVSYGP VTDVAFREWL RARYGDLSRL
NEAWNTTFWS QVYGDWRDVH APQATQYLPN PAHVLDFKRF SADLLLERLR DQVAIVRELS
PGVPVTTNFM LPSWNHYDQW AFARELDVVS IDHYLDDPGP SGEVHAAFGA DLARSFAGGA
PWLLMEQATS LVYDYDGGRM LVKKPGRMRR NTYQYLARGA MGSLFFQWRS PVVGAEFFHS
AMVPHFGADS RLFREIEQLG RELPRVAELA MAPTDGPVVD SRVAIVWSAD AWWAADTRAM
PSADVGFLPA VRRVHTTLWE LGVVADVVAP DGDLSRYDVV LVPSLLAVSD RDAAAFADFA
HSGGHLAVWH FAGSTDERLH VRQGSYSGAF ADLAGVRVEE HVPLRDGERV TLSDGSTAEA
WTERLHLSGA TAVCAYTDDA HPVVGPGSPA ITERPLPGGG RVHYLSTRLA AGDLGRHLGR
IVRAAGVEAR GFTGLEVVHR RAGTSSYLVA INHSQEDGTL EAHGTDLITG RVAAGNVVVP
AGDVAVVRLE ENT
//
