ID U7V8E6_9FUSO Unreviewed; 983 AA.
AC U7V8E6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HMPREF0202_02133 {ECO:0000313|EMBL:ERT67977.1};
OS Cetobacterium somerae ATCC BAA-474.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Cetobacterium.
OX NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT67977.1, ECO:0000313|Proteomes:UP000017081};
RN [1] {ECO:0000313|EMBL:ERT67977.1, ECO:0000313|Proteomes:UP000017081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT67977.1,
RC ECO:0000313|Proteomes:UP000017081};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERT67977.1}.
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DR EMBL; AXZF01000094; ERT67977.1; -; Genomic_DNA.
DR RefSeq; WP_023051665.1; NZ_KI518072.1.
DR AlphaFoldDB; U7V8E6; -.
DR STRING; 1319815.HMPREF0202_02133; -.
DR PATRIC; fig|1319815.3.peg.2053; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_0; -.
DR Proteomes; UP000017081; 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:UP000017081}.
FT DOMAIN 710..980
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 983 AA; 114789 MW; 7927509AB6CC62D1 CRC64;
MDNLHNPRVF KINRLSAHSN HKYEGLNIEW KKCLNGIWDF SYCNTPNWAK IQVPGHMELQ
GYGEPQYVNT MYPWDGRENL EPGEVPKEFN PFGIYKRNID IPKDWKNRPV YISFQGVESS
LELYCNGEFV GYSEDSFTPS EFELTKYLKN ENNEITVKVY KWCSGSWLED QDFWRLSGIF
RDVYLYSIPD VHVKDMFITS ELVNNFKKAT LKNILKIQSY KEAIVDIEME LIDKAEVIFK
VEEKNIKIEK ELKLELNKKV ENPKLWSAEK PNLYVVKVLI KDTKTGDIIE ECWQKFGFRK
FEISDKIMKI NGERIVFKGV NRHEFNCYKG RAVTEEDMIW DIKFLKANNF NAVRTSHYPN
QTRWYELCDE YGLYVIDEVN LETHGTWQIL GQPCPEKVIP NNNPEWLENI IDRAKSMFER
DKNYPSVVIW SCGNESFGGE NLFKMSEFLR SLDNTRVIHY EGIFWDRRYD KTSDMESRMY
AKVYEIEKYL QETPEKPFVL CEYSHAMGNS NGGLHKYTEL ERKYPMYQGG FIWDYIDQSL
MKKDSFGKEY LAFGGDFGDR PTDYNFCVNG IVYGDRKPSP KVQEIKQLFS DYKINVEEKS
FTIINESLFT NCSEYDTKIK LFKNGIKIYE ESLECNVKPL SEKSFKLNLP KVKEHGEYTI
EVSLNLKEDR FYALKGHEIC FGQKIYKIEK KVKEKLEGKP TFINGGFNLG IKTKKMELIF
SKAYGGLISL KFGGKEFVDG VVMPNFWRAS TDNDRGNKMP FRYAQWKLAS MYAKMVDVKA
LERENSVEIR AKYELPTNPS SVCEIIYEGF VNGKLKISME YNGVKGLPEM PLFGMSYKVP
KEFSEIKWYG MGPEENYIDR VHGAKLGIFE TDVNKNMSEY VIPQECGNRI GTRWAEITNK
MGVGIKVSSE ETFEFSALPY TVNEIESAYH HYELPKSHCT ALNINKIQMG VGGDDSWGAP
THDEYLIPSD KKYLFSYIIE SNM
//
