ID G6AVX2_9BACT Unreviewed; 1121 AA.
AC G6AVX2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=HMPREF0673_00767 {ECO:0000313|EMBL:EHJ41433.1};
OS Leyella stercorea DSM 18206.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Leyella.
OX NCBI_TaxID=1002367 {ECO:0000313|EMBL:EHJ41433.1, ECO:0000313|Proteomes:UP000004407};
RN [1] {ECO:0000313|EMBL:EHJ41433.1, ECO:0000313|Proteomes:UP000004407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18206 {ECO:0000313|EMBL:EHJ41433.1,
RC ECO:0000313|Proteomes:UP000004407};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:EHJ41433.1}.
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; AFZZ01000069; EHJ41433.1; -; Genomic_DNA.
DR AlphaFoldDB; G6AVX2; -.
DR PATRIC; fig|1002367.3.peg.609; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_10; -.
DR Proteomes; UP000004407; 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; 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1121
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003485319"
FT DOMAIN 825..1100
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1121 AA; 126440 MW; C225B76692F1538B CRC64;
MKKTLLLVAV AALVCSGTAY GQRKAKRQAK KNVPTIVHAV ETKDIAEVVD SWVENEQKFE
DQKLPAHATF IPYSSTSQMM LDKCYAKPWL TPERADYLLL NGEWKFRYTA DWKQGKPEEK
DFYGDNADVS AWDNIKVPLN WEMAGYDVPV YNNVGYPFHN DPPRIKAMDD NFDKNPVGSY
RRTFNLPEGW EKDKRVVLHF DGACSAIVVW VNGKYAGFSE GANTDAEFDV TALVRKGENN
VSVRVYRWSD GSYLEGQDMW HLAGIHRDVY LMATPKVAVS DHYITSQLGE GYTAGSMNVE
LTVDNSLKQS ASKTLEVELL DPAGQLVAKK LQAVALTAKD AQKTVSIDFD GLTDLKLWSS
EHPWLYTVIV RQMGNAGEEM VFSTKYGFRS VEQKGNLIYV NGKRVYFKGV NTQDIHPLLG
HAIDVKTMLR DVELMKKANV NTVRTSHYPR QAKMYAMFDY YGLYCMNEAD VECHGNQSIS
DMPSWEGAYV DRTARMVLRD RNHPSVVFWS LGNESGGGCN FQATYDCVKR LLPRRDAWVH
YEGYNHGEKY SDFGSDMYPV VSKVVEQRDG LNNKPYFICE YAHAMGQAVG HLQEYWDVIE
NSNGIVGGCI WDWVDQGIYD TRRIKAGEPL TDPKTGIPYY TSGYDYTKMN RGDYGFQGDF
MSNGIITPGR EWTAKLDEVR YVYRDVDFVS FANHKLTLKN KFAFTDLRNY QLIWSISGRG
EGESNLAHGT VKDLQCKPGE TCVVEIPYDV NVPADKEIII TFKLKVKDKT AWANRAHVIA
AQQFCLTADA AANCPSVADP TYVQHNHIAL PAISEKGKLK VKGNSVEGKN FSIKFDTDGT
IAEWTYEGKQ IVMPSAGPDF NGFRRIANDN ISLGATGGVA ENENKEEGAL SGQKTLVKAP
KKQGNNVLVE TAVSNGKDTH HILYTIYPNG EVDMRVAFNN SSEETRRVGI TMQFAPGFES
VLYYAKGPRS NYIDRQRGSL LGWYRTSVDK MFEQQSAPQT MGDRQGLREM TLKNSGNGVG
LNMKVEGQLA FSLSHYDDQQ FNYDVFYGGK HPYDLTRSEQ VFAHFDFWQR GIGNHSCGGD
SCLPQFKTPT GEHVVTMRFA PYTFNPKTRI LPKMQRIEMN R
//
