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Database: UniProt
Entry: C0W6J3_9ACTO
LinkDB: C0W6J3_9ACTO
Original site: C0W6J3_9ACTO 
ID   C0W6J3_9ACTO            Unreviewed;       914 AA.
AC   C0W6J3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=HMPREF0058_1487 {ECO:0000313|EMBL:EEH65517.1};
OS   Actinomyces urogenitalis DSM 15434.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=525246 {ECO:0000313|EMBL:EEH65517.1, ECO:0000313|Proteomes:UP000004778};
RN   [1] {ECO:0000313|EMBL:EEH65517.1, ECO:0000313|Proteomes:UP000004778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15434 {ECO:0000313|EMBL:EEH65517.1,
RC   ECO:0000313|Proteomes:UP000004778};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA   Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA   Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA   Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA   Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA   Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA   Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA   Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA   Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA   Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL   Submitted (JAN-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:EEH65517.1}.
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DR   EMBL; ACFH01000109; EEH65517.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0W6J3; -.
DR   STRING; 103621.GCA_001067145_00794; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_0_2_11; -.
DR   Proteomes; UP000004778; 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   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   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:UP000004778}.
FT   DOMAIN          629..902
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   914 AA;  102876 MW;  3BFC51B34C2B54ED CRC64;
     MWQLDGFGKL QYTDEGFPFP VDPPHVPSDN PTGVYQRLFT YEPEQAGEQV LLHLGGVESY
     VEVYLNGSYV GMSKGSRLAA EFDLTGLVTL GPNLVVLCVA QFSDGTYLED QDMWWASGVF
     RDVWVERRPP ARLEDFTVTT HLVRERAQVD VACWTQGAAR VECEIWDHGT LLAQGWCTSE
     GSVRLCVDAP RTWSPEDPYL YDLRLRVWDG QTQTEVVPYR LGLREITIRD GLMYLNGRYF
     MMHGVNRHDF DPRRGRAVSA ERIRADLELM KRHNINAVRT SHYPNDPRFY EMCDELGLMV
     MAENDLETHG FALCGDLERL TDDPGWQPAF VDRIERHVVA QRNHASILIW SLGNESGDGC
     NIAAMYERAK ALDPSRPVHY EEDRDGRIVD VVSTMYSRVS QMNDLGERPC GKPRVLCEYA
     HAMGNGPGGL SEYQEVFRRW PSIQGHFVWE WIDHGVLQVD EEGRQYYAYG GDFGDEPNNA
     NFCIDGLVFP WLEPSPGLLE YKQVICPVGV ELSDGQVRVT SRRWFTDLSD VELEVGLRDD
     GVLLASQRVR PGALLPGESL TLALSPELAA RHARGEAILS ASVWGTAIAG QAPCELGVFQ
     QVLTPWSPAT LTASSHEPVT VLSRGEHLDV ERAGTRLTFD RVSGQLCSWQ VDGIELLAGP
     PEVGLWSPVI DNHRREAETL WWPRNLHLMS RSLRQMSWHE AGDAVVVECR ERIGTPSYDI
     AMTVDLRWTV RPDGGVELAV QGRAEGDYDD LIPRIGLTWT LSEDLREIEW YGRGPGESYP
     DSWTASPIGL WESDVESMLT PYVLPQGNGN HQDVRWVQAR AGDGHGLQVR ACSSDLLAFS
     AWPCTARDLD QARHLNDVPR RGPVTLNVDH KVLGLGSNSW GSEVLERYRL RFTDFSFRLM
     LEPVRGGHTD AAHH
//
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