ID G2SXE2_ROSHA Unreviewed; 1059 AA.
AC G2SXE2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=RHOM_10950 {ECO:0000313|EMBL:AEN97299.1};
OS Roseburia hominis (strain DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=585394 {ECO:0000313|EMBL:AEN97299.1, ECO:0000313|Proteomes:UP000008178};
RN [1] {ECO:0000313|EMBL:AEN97299.1, ECO:0000313|Proteomes:UP000008178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16839 / JCM 17582 / NCIMB 14029 / A2-183
RC {ECO:0000313|Proteomes:UP000008178};
RX PubMed=26543119; DOI=10.1128/genomeA.01286-15;
RA Travis A.J., Kelly D., Flint H.J., Aminov R.I.;
RT "Complete genome sequence of the human gut symbiont Roseburia hominis.";
RL Genome Announc. 3:E0128615-E0128615(2015).
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}.
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DR EMBL; CP003040; AEN97299.1; -; Genomic_DNA.
DR RefSeq; WP_014080317.1; NC_015977.1.
DR AlphaFoldDB; G2SXE2; -.
DR STRING; 585394.RHOM_10950; -.
DR GeneID; 77459773; -.
DR KEGG; rho:RHOM_10950; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_9; -.
DR OrthoDB; 9762066at2; -.
DR BioCyc; RHOM585394:G1H02-2184-MONOMER; -.
DR Proteomes; UP000008178; Chromosome.
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:UP000008178}.
FT DOMAIN 780..1057
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1059 AA; 120745 MW; E8FB8D5C33160A2E CRC64;
MGEFLFERLS DPEYYEENRV AAHSDHVAYR NWDEADVWLD PLGRKSSFRL FLDGSWKFHY
ARNYEQTIHG FEKPEYDCRG WDDIRVPAHI QMEGYDSPQY ANTQYPWDGR EDVWTDEMPT
KFNPVASYVK YFTLPESFLG ERVFISFQGA ESGMALWLNG AYVGYSEDSF TPSEFELTPY
LKDGENKLAV QVFKWTIGSW CEDQDFFRFS GIFRSVYLYM IPKTHLCDIK IRPQVAENLS
CGTLELDLRS CGSGSVRIQL VERGRLDLAE SRYETPEGTE VFALEEKMEG TLHVSREVAD
VKLWSAEEPY LYELRMEVYD AAGALQEVVA SKIGFRRFEM KDGLMLLNGK RIVFKGVNRH
EFSSLTGRVV SMEETLTDVV TMKRNNINSI RTCHYPDNIG LYELCDIYGL YMIAENNMES
HGSWDAAAMR KIADPRTIVP GDNPKWEARM LDRVNSCYQR DKNHPAVLIW SCGNESYGGS
VIYQMSEKFR ELDPDRLVHY EGVYNDRRYN GSSDMESQMY PPVERIVKNL AEQKEKPFIC
CEYTHAMGNS CGAMHKYTDL TDTEPRYQGG FIWDYIDQSI TKKDRYGKEF QAYGGDFLER
PTDYNFSGNG ICYAKGRAES PKMQEVKFNY QNISVSFTED GFTVKNKNLF TDTAEYDCIL
LLEKNGVAAG RRKIALSVAP LSEKTFVLEE LEGCMALADE LEHAGKEAGA EYALTVSFVL
RGELLWAKPG HEIAFGQKIF AAKSPANGGT IGDAAAEYEG KCVTNRKAGL QIIRGKWNLG
VKGENFDVLF SYNSCGLVSY RYMGKELIEK IPMPNFWRAP IDNDCGSRMQ GRMAQWKIAS
MYAGMSSKGM FDYEEPVVRE AENSVSITYT YLLPTTPQAK CRVTYTVTPD AYVQTELTYD
PVEELGDMPE FGMLFKLNAD YDRLEWYGLG PQETYADRRC GAKLGVYKNR VADNMAQYLV
PQECGNKVGV RYAKVTDARG RGMLFTGDEL SFSALPYTPH ELENAMHAYE LPEVHYTVVR
VALAQMGIGG DDSWGAPVHP EYHIDVTKPL ALRFGFRGI
//
