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Database: UniProt/TrEMBL
Entry: S0EWR0_CHTCT
LinkDB: S0EWR0_CHTCT
Original site: S0EWR0_CHTCT 
ID   S0EWR0_CHTCT            Unreviewed;       937 AA.
AC   S0EWR0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Beta-galactosidase (EC:3.2.1.23) {ECO:0000313|EMBL:CCW36355.1};
DE            EC=3.2.1.23 {ECO:0000313|EMBL:CCW36355.1};
GN   ORFNames=CCALI_02561 {ECO:0000313|EMBL:CCW36355.1};
OS   Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC   Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC   Chthonomonadaceae; Chthonomonas.
OX   NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW36355.1, ECO:0000313|Proteomes:UP000014227};
RN   [1] {ECO:0000313|Proteomes:UP000014227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23976 / ICMP 18418 / T49
RC   {ECO:0000313|Proteomes:UP000014227};
RA   Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA   Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT   "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT   from the Armatimonadetes phylum (formally candidate division OP10).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; HF951689; CCW36355.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0EWR0; -.
DR   STRING; 454171.CP488_01530; -.
DR   KEGG; ccz:CCALI_02561; -.
DR   PATRIC; fig|1303518.3.peg.2661; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_0_1_0; -.
DR   InParanoid; S0EWR0; -.
DR   OMA; EEGWFYE; -.
DR   OrthoDB; 9758603at2; -.
DR   Proteomes; UP000014227; 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; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR048230; GalA-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
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   NCBIfam; NF041462; GalA; 1.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-GALACTOSIDASE (EUROFUNG); 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 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; 2.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CCW36355.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCW36355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014227};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..937
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004496470"
FT   DOMAIN          213..339
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          347..456
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          464..641
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          760..817
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          830..931
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   937 AA;  103661 MW;  08E25854393CADFA CRC64;
     MKVQKALVLL PLAVALSLPS PAFATHRARA ESPFGERQKI LFDANWRFFR EPTPHLEKTV
     PITDWVYLPI EEGAGDARVL ADPNLDTSAG GWKPVKTGTD VFEGRVGFAW FRTTLPPIAP
     PPKGYSLYLL FENVDDNGTV YLNGKKLYYH EGYGEPFVVP LAEAWRSNGP NLLAVQVDNA
     GGGPGGILGD VFLGYAKGAD IGSGAAQPDF NDSSWRIVHL PHDYVIEGRF DPKASVSHGF
     LPTPPAWYRK TFYLPASDRG KSLWLYFEGV FRDSDVWLNG KFLGNHPSGY TSFFYNIAKA
     AHFGGKNVLA VHVDPGNYEG WWYEGGGIYR HVWLIVTNPV HIAQWTTFVN PQVVGDDVEH
     PAMAQVNVHT TVENDTDAEA ACRLQFRVLD AENHLVAQTD STVSIPPNGT RKVAVLLPLH
     APHLWSLESP YLYKLQISVL RDGRIVDGNE TNFGVRTIRF DPNQGFFLNG KHVELQGTCN
     HQDFAGVGIG MPDSLLEWRI RKLKEMGSNA YRCSHNPPAP ELLDACDRIG MLVMDENRHL
     GDVYTPKTPP NAPYSDLSDL ASMVRRDRNH PCIILWSLCN EEGIQGTPAG ERMGAAMKKV
     VESLDPTRPV TAAMNGGWGY GLSHVLDVQG INYSYGVYDS FHQSHPDFPI VGSEIGSDVS
     DRGIYANDPA KGYVSAYNNA ENTWKSVATH PFVAGGFVWT GFDYKGEPSP YGWPCVNSHF
     GLMDLCGFPK DDYYYYKAWW DQEHPLVHLF PHWNWQGKEG QPIDVWCYSN CDAVELFLNG
     KSLGKKEMPK YWHVEWHVPY SPGVLEARGY RNGQVVATDR VETTGPPAAI RLTTSTPTIK
     ADGEEVGIVE VAIVDAQGRV VPTADNLVHF RVRGAGSIAG VGNGDPSDHE PDQANYRHAF
     NGLCLLVVRA GNRPGSIEVE ATSEGLRSAH LRLEAVR
//
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