ID D0GIW0_9FUSO Unreviewed; 1045 AA.
AC D0GIW0;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=HMPREF0554_1281 {ECO:0000313|EMBL:EEY35939.1};
OS Pseudoleptotrichia goodfellowii F0264.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Pseudoleptotrichia.
OX NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY35939.1, ECO:0000313|Proteomes:UP000004226};
RN [1] {ECO:0000313|EMBL:EEY35939.1, ECO:0000313|Proteomes:UP000004226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0264 {ECO:0000313|EMBL:EEY35939.1,
RC ECO:0000313|Proteomes:UP000004226};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (OCT-2009) 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:EEY35939.1}.
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DR EMBL; ADAD01000030; EEY35939.1; -; Genomic_DNA.
DR RefSeq; WP_006806437.1; NZ_ADAD01000030.1.
DR AlphaFoldDB; D0GIW0; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000004226; 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:UP000004226}.
FT DOMAIN 760..1041
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1045 AA; 121961 MW; F406C75565DFE1CA CRC64;
MNINNLENLN ILGVNRIKPR STFFGYDSLE KAESYNRIFS KGFKLLNGNW KCLYSEYPDN
FPDNFFTPEF DDTDWDTIYV PSNWQMEGYD KPWYTNVQYP FPVNPPHVPS LNPSMVYRRK
FYMSALDLKN VQYLKFEGVD SAFHVWINGK YIGYSQGSRI PSEFKINDYI IQGENLICVL
VHKWNVYSYL EDQDMWWLSG IFRDVYITSE PEIHIYDIFA KTSLDETYKN GILDLEVDII
NNKNSKDLSI EILLKDKSTD YFLIKENSDL DSSVKSNESG IKKYNFHYEI KNILKWSAET
PDLYELYITL KEKDNVLQIV PLKTGFKKIE IKDGIMLFNG KYIMLKGVNR HESHPVYGRS
VRIEHMIQDL KLMKEHNINA IRTSHYPDDP KFYDLCDEYG FYVIDEADLE THGFEFVNKR
NYLNNLEEWK AAFKDRAERM VERDKNHPSI IMWSLGNESG YGKNHAAMTD YIKDRDDSRL
VHYEGETREI FESTDNGLPD RDPESSDVHS TMYTPIEILE KVAKLNFLKK PHIMCENLHA
MGNGPGGIKD LWELLYREKR LQGGFVWEWC DHGILRTLEN GEKYYAYGGD FGDTPSDSNF
VIDGLVNPDR TPSPALAEYK KAIEPIKMFA LNSEKTKYEV ENRYDFINLN DFICNYEIKT
NGKTVQTGYL ENININPSKK AQFKINIGNS ILNKDGDYYI TFSWKIKKNI GLLPAGTELA
FHQEKLSINK NTEKTSCDDE IYLKNAPDIF NIVENKNELE ISLFNKKIVF DKNTGKISAY
YHNGINIFKD GISLNLWRAP IDNDILEIEE FGAKKALNHW KEKCVNLVQH SLRNFKISEK
TDDYIVIDVQ AEVAPAVLDW GYNVHYKYKI DRKGTVTLNI TGKTYGNVPE TLPRIGVVMN
LDKLFTDVHW LGLGPQESYI DSCSSVKFDL WHKKIEEMHT PYIFPQENGN RHNVKSFSLD
SEKNIGIYFE SLDNKFDFSV SEYTIENIEK AKHTYDLKKE NFLQLKIDME QYGLGSASCG
EETLEKYRLY CKDFEFSFKF CTFSK
//
