ID A0A0U1NYS6_9BACI Unreviewed; 1060 AA.
AC A0A0U1NYS6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN Name=lacZ_2 {ECO:0000313|EMBL:CRK83166.1};
GN ORFNames=BN000_03125 {ECO:0000313|EMBL:CRK83166.1};
OS Neobacillus massiliamazoniensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1499688 {ECO:0000313|EMBL:CRK83166.1, ECO:0000313|Proteomes:UP000199087};
RN [1] {ECO:0000313|Proteomes:UP000199087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LF1 {ECO:0000313|Proteomes:UP000199087};
RA Urmite Genomes;
RL Submitted (MAY-2015) 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|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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; CVRB01000003; CRK83166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1NYS6; -.
DR STRING; 1499688.BN000_03125; -.
DR Proteomes; UP000199087; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000199087}.
FT DOMAIN 783..1058
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1060 AA; 122163 MW; BCD93AAFD9F65BF4 CRC64;
MESTRNSFLN KEGNVMKEIE YGWLEDFQKY EENKEKGRCL LLPHRSKESC LHEEASPYKL
SLNGEWRFLY HINPNTLPHG ITEDEFDDSL WDLITVPSVW QLEGYGKPVY LGASYPYPVD
TTPEKIPHIR QDLNEVGIYK RDFTIPESWN GRQVFVHFGA AKSAMQVFVN GKEVGKSKGS
MTPAEFCLTP YLRPGKNSIV AIVYRFSDAT YLENQDMWSF SGIYREVYLF SEPSVRLRDC
WVQSDFNEDF SCSFNKLFFE AQNFTNEPQT LHLSAMLYKD GQTYPLGKCR LVVAPGSCSA
ECIESDFARP LLWSAETPHL YQILLETRTE QSAAEYKAFT YGFRKIEIKE NVLYVNGKNI
KLKGVNRHDF DPDHGWAVPR ERYLQDVLLL KKNNINAVRT SHYPDDPYFY DLCDRYGIYV
MDECDLETHG VRDYIPQDNM DLVAPCSDRL ERMIYRDRNH PSVIIWSTGN ECGAGAVMQE
MYKIAKQLDP TRLVHYESDY RPSCSDFSSR MYFPPNALEK MALNEEVTPQ DVGVGGQSIP
QEIFPFMQKR FTHRVEDIAN RPIILCEYAH CLENSMGNFQ EYVDVINRYD NISGAFIWDF
CDQSIRQFVN GQERFLYGGD FDEGASNTYF CANGIVQSTR EPHPALYQVR KSYQNILMFT
TDSAFQVHVR NENRFISLSD YLLVWRIECE GVKIAEGNDQ NFNLEPMQSG VWRPDYDFAK
LPSGECFLTV EFRLKEDCEW ARQGYVVAYE QLLIQKAETQ LLSVQEGEKN AALVCEEQGR
TIKFSNDVVS IRFDTRNGFI NSLAFHGNDV ISTPVVPCFY RSLTDNDRGM ANFFPPLGLM
GVPGMQWKDI HKKLKLINFS YETKGSTVTV RSCYTHRLLK SLQLIYQIDT AGKVELVMTV
IPAESPFRIG FTTQIAHSFS QYEWYGRGPF ETYCDRKSAA LISQYQSNID ELQQQYMRPQ
ENGNRTDIRF LKVKNAAGDG FCVRDKSGNG FNFSAHPYTL DDLDKAGHIF ELPSRETVSL
YLDGYMCGVG GDSPGFAFLK HPYYIHADTE YTQKIEISPL
//
