ID   E7MQ55_9FIRM            Unreviewed;       779 AA.
AC   E7MQ55;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Putative beta-galactosidase {ECO:0000313|EMBL:EFW23775.1};
GN   ORFNames=HMPREF9430_01580 {ECO:0000313|EMBL:EFW23775.1};
OS   Solobacterium moorei F0204.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Solobacterium.
OX   NCBI_TaxID=706433 {ECO:0000313|EMBL:EFW23775.1, ECO:0000313|Proteomes:UP000004097};
RN   [1] {ECO:0000313|EMBL:EFW23775.1, ECO:0000313|Proteomes:UP000004097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0204 {ECO:0000313|EMBL:EFW23775.1,
RC   ECO:0000313|Proteomes:UP000004097};
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-2010) to the EMBL/GenBank/DDBJ databases.
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:EFW23775.1}.
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DR   EMBL; AECQ01000031; EFW23775.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7MQ55; -.
DR   STRING; 706433.HMPREF9430_01580; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_5_1_9; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000004097; Unassembled WGS sequence.
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; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 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.
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:UP000004097}.
FT   DOMAIN          39..152
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          158..244
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          249..520
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   779 AA;  88947 MW;  8EEFB43CC381F9DF CRC64;
     MISRMNNDWE YIDHWSDAFI LEGEAEEVVR LPHTVQELPL HYADADSYQK VVGYRKKLIF
     PSSLKGRRHF IRFDGSAHES TVYFNGKEMY VHACGYTAFT VELTDEIRFD EENLLTVKVD
     SRESLNTPPF GFVIDYLTYG GIYRDVWLYD KPTYFIKDVF VMTKSLDTVS VSIQTEGTVP
     ADTYHVKIFD FKGEMLAEEI VPINKQQIQI PVSNIHAWSA ESPTLYRCVV ELGEDSYETN
     FGFRTIRFDQ NDLYINNQKV FLIGLNRHQC YPYIGYAAVD SLQEEDVRIL KEELHVNAVR
     TSHYPQSQSF IDACDRYGLY VFTEIPGWQH IGDDTWKQQA IQNTKDMVLQ YRNHPSIILW
     GVRINESLDD DALYTKTNQV ARDLDPSRPT AGVRYLTKSH LLEDIYIFND FSHHGDNKGA
     LSKSEVMVDT HHPLIISEAN GHMFPTKSFD TQVRRQEHAL RHARVFSDAM ADGQHTGVFQ
     WCMFDYATHK DFGSGDRICY HGVMDSFRNP KLAASVYASQ QDEEPILEIS TSMDIGDYNA
     GNLPDFFAFT NADEVRLYKN NQFVSSFATS VYSGLKHGLI RIDDTIGELL VENEHYTSKQ
     ADDIRKCLLA SKKYGSNLPL RYRLLYAKIM FQYKMSYSDG VALFGKYVSG WGSDSITWRF
     DAIKNGEVVK SIIKCPSAKL HLSYQVSRKI LIEGDCYDMS AIRIQVKDEY NNPASYAQFP
     LSFITTGPIE IVGPKTVVAE GGMTGTYIKT TGEEGEAILT ISAPDCSSIT IHFTVKKES
//