ID D4KT13_9FIRM Unreviewed; 633 AA.
AC D4KT13;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=ROI_31500 {ECO:0000313|EMBL:CBL10015.1};
OS Roseburia intestinalis M50/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=657315 {ECO:0000313|EMBL:CBL10015.1, ECO:0000313|Proteomes:UP000008807};
RN [1] {ECO:0000313|EMBL:CBL10015.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL10015.1,
RC ECO:0000313|Proteomes:UP000008807};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Roseburia intestinalis M50/1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL10015.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL10015.1,
RC ECO:0000313|Proteomes:UP000008807};
RA Pajon A.;
RL Submitted (MAR-2010) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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; FP929049; CBL10015.1; -; Genomic_DNA.
DR RefSeq; WP_006859544.1; NC_021040.1.
DR AlphaFoldDB; D4KT13; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GeneID; 61433743; -.
DR KEGG; rim:ROI_31500; -.
DR PATRIC; fig|657315.3.peg.331; -.
DR HOGENOM; CLU_002346_3_2_9; -.
DR Proteomes; UP000008807; Chromosome.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 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}.
FT DOMAIN 42..227
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 229..337
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 341..630
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 633 AA; 73581 MW; 0E1A8E499F197336 CRC64;
MNADMKWLDN PEVFRVNQLD AHSDHCYYMD YADMEKSENP LMQSLNGQWE FAFSKNVMDR
PENFYEENFD ASSFDKIMVP GHIELAGYDK IRYINTMYPW EGKEYHRGAY SMESTGDEAG
MFSEAEYNPV GSYIKRFDLS EQMREKKIRI CFEGVEEAMY LWLNGQFVGY AEDSFTPSEF
DLTPFIREKG NVLAVQVHKM STAAFLEDQD FFRFFGIFRN VTLKAVPEVH LEDVWFQPTL
NKDNISGRVS VKMKVSAPEG KKVSAHLVLK DRENNQVAED NITLEEKAGS LVGVIDTEVG
SVKAWDNYCP YLYHAYVELR GEDGEILEII PYDIGFRRLE MIDKVIYLNG KRLVITGVNR
HEWSAKTGRS ISMDEMTADI DCMIRNNINA VRTCHYPDQI PWYYLCDKAG IYVMAETNME
SHGTFQKLGA IEPSCSVPCS IPQWREAVVD RARSNFETFK NHTAILFWSL GNESYAGDDI
EAMNTYFKEK QDGRFVHYES SFYDRNYEET ISDVESRMYA KPYEVEEYLN NNPKKPYLLC
EYMHDMGNSM GGLGTYMKLI DKYEMYHGGF IWDFIDQALL VKDEVTGKEV LRYGGDFDDK
PSDYEFSGNG IVFADRKEKP AMQEVRYYYG LYR
//
