ID A0A0N0K5T4_9PROT Unreviewed; 1070 AA.
AC A0A0N0K5T4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, 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 ORFNames=IP70_23890 {ECO:0000313|EMBL:KPF81435.1};
OS alpha proteobacterium AAP38.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF81435.1, ECO:0000313|Proteomes:UP000037884};
RN [1] {ECO:0000313|EMBL:KPF81435.1, ECO:0000313|Proteomes:UP000037884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP38 {ECO:0000313|EMBL:KPF81435.1,
RC ECO:0000313|Proteomes:UP000037884};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF81435.1}.
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DR EMBL; LJHR01000048; KPF81435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0K5T4; -.
DR STRING; 1523418.IP70_23890; -.
DR PATRIC; fig|1523418.3.peg.3533; -.
DR Proteomes; UP000037884; 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}.
FT DOMAIN 770..1049
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1070 AA; 119209 MW; 5D30C17D6764F10B CRC64;
MALVLPAAAQ EAVVPNMDPV QVDPRRPDWE NPAVNERGRL PASATMFGYE SRDLALGGDR
TKSDRHLSLD GQWHFHFTPS ANSLPDGFER SDYDVSTWPL IKVPSMWQAE GYDQARYNNA
TYPFPANRPL IPHETNPVGS YRRDFNLPAH WSGQNVILHI GAAGAAYYVW INGQKVGYAE
DSKLPSDFDV TPYLKPGRNM VAIQVFRWAD GSYMEDQDFW RVSGIERSVR LYAVPQVRVR
DLFVRAGLDK DYRDGTLSTD IAITPGSKAA SVRLTLLDGA REVLVREAKV RAGKAERLVT
LTATIPGVQP WSAETPKLYT ALVELRDADG NLLQAVPQRI GFRTVEMKGG QVRVNGKPIT
IRGINRHEHD PETFHVISEA SMRRDIELMK LNNFNAVRTS HYPNDPRWYE LADEYGLYVM
DEANNESHAY LGLSTRYPEF REKLAMGFDP AWEEAHISRV MNMVERDKNH PSIIFWSLGN
ETAVGPSFEK AAAAARKRDP GRLLSFLGWG TIAWEHRPNA YVDIYAPMYD DIEKMVDWAT
DPSRTQPMIQ CEYAHMQGNG GGNFKDYWDT IYRYPDKLQG GFIWDWVDQS MYRYTKDGRR
YWGDGGEYGP NPGGDIEFGD GLIQPDRTPN PHLYEVQKVQ SPIQFDGFDP ETGRVTVRNR
HDFLDLSGFA FDWVLEEDGV AVARGDLPPL NTAARAATDV IIPIPSLPRK PGAEYLITVR
VIAKEGTVPL VPAGHVVGWE QFTLAAPTAA TTRNVAQGTV KIDEREGHVR LTAAGAVLDI
DAKTGLLTGY SRDGKHLLAG GTPNFYRAET DNDLATGTLS VVLVGREYAW KTMTERRQLR
NLAVERGTAG GTVTVEHMLG GGAARFTTRY QMRGDGTVQV TGEMVPLKDD LPPPTRIGLW
FTTNPALSTV QWYGRGPHES YVDRKTSAAI GLWRGPVADQ NHDYMRPQDT GNKVDVRWLE
LIGGQGAGVR VIGDTPLMMN ALAFPYTDLY RRPPGTWKST DIVPHGDGTL LIDAAQSGVG
GDTSWDAVGQ PHMQYRTKLA VTRFSFRIET FTGAGTQADK AKPAVRDAAH
//
