ID R5XDE8_9FIRM Unreviewed; 1019 AA.
AC R5XDE8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=BN695_01146 {ECO:0000313|EMBL:CDA12895.1};
OS Anaerotruncus sp. CAG:528.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=1262700 {ECO:0000313|EMBL:CDA12895.1, ECO:0000313|Proteomes:UP000018024};
RN [1] {ECO:0000313|EMBL:CDA12895.1, ECO:0000313|Proteomes:UP000018024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:528 {ECO:0000313|Proteomes:UP000018024};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDA12895.1}.
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; CBBE010000040; CDA12895.1; -; Genomic_DNA.
DR AlphaFoldDB; R5XDE8; -.
DR STRING; 1262700.BN695_01146; -.
DR Proteomes; UP000018024; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW Reference proteome {ECO:0000313|Proteomes:UP000018024}.
FT DOMAIN 741..1018
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1019 AA; 116826 MW; D523A67A563F4647 CRC64;
MERNFVDGYL EWQSDPEITG VNKLPQHANL MPYSDFEEAK KCNRIESSCC RLLNGKWKFK
LYKNYAYRPT DFAQPHYDAH NWDSVIVPGS WTMQGYDQNQ YCNVRYPWEG HEDICPPNAP
TKHNPVGCYL KKIHINKSVL SKRVVICFDG VEAAFYLYVN GERVGYSESS FNRSEFDISR
YLVEGSNVIG VEVYRWCTGS WLECQDMWRM AGIFRDVYIY TTEREYIRDY IINAVPSETL
ADGYFDVTVK TNGAYEGLSI DLSILDENGE TVAIDSRYAN EDNVTPLKAI VTGAKLWSAE
APNLYTLVIT LKNNGIPTEY LSTKFGFRKV EIKDGIIRIN GERVVFKGTN RHEFDCRLGR
VMTEETMLKD ILLMKQNNIN AVRTSHYPNC VRWLELCDEY GLYVIDENNM ESHGTNRSRI
IGCPQIPGSR PEWEKACMER IKALYNRDKN RTCVVCWSLG NESLGGEIPK KMYKWIKEQD
PSRFVHFECA GDPNEKNLSD VQSHMYAKPW DCEEYAVTQR DGRPYILCEF THAMGNSCGS
TQEYTYLWDK YPCLQGGFVW DWVDQAIMTT DENGTEYLAY GGDFGDEPND GHFCGNGLLF
ADRTPTPKLY EIKKLYQNVD FKAIDAEKGV IEIKNKFLFD DLSGCELYWC QCSDKGVLRE
GTVDVKIKPG TKEIVDLELN RITNTECYLN LALRTKEDNA WSKAGHIIAE EQFVINEFEN
TYDELEPGEE LVVADTYGSL RIFTEDINIR FERRERNQLY SVKVGGEELL AAPVRLNFWR
ALTDNDRGSR AGSRLGCWRD AGNAPGIYNN TKFSIEGYKI LENGKKVIVT CGATVCTQPE
SKAIMIYTIT SNGIEVDMQF RAGEGLPEIP EVSMLFELPG DFENITYLGA GPFENYIDRK
CAAQIGLYND TVTNMYTDYL KPQECGNRTG VRYATLVGNK KAITFIAEPV MEFNASHYLP
MQLENAWHKK ELPQSDKTIV RVIARQQGVG GYDSWGATCN ELYMNKSDKL YRLKFQIRF
//
