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Database: UniProt
Entry: C4GDQ0_9FIRM
LinkDB: C4GDQ0_9FIRM
Original site: C4GDQ0_9FIRM 
ID   C4GDQ0_9FIRM            Unreviewed;       617 AA.
AC   C4GDQ0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Glycosyl hydrolase family 2, TIM barrel domain protein {ECO:0000313|EMBL:EEP27529.1};
GN   ORFNames=GCWU000342_02224 {ECO:0000313|EMBL:EEP27529.1};
OS   Shuttleworthia satelles DSM 14600.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Shuttleworthia.
OX   NCBI_TaxID=626523 {ECO:0000313|EMBL:EEP27529.1, ECO:0000313|Proteomes:UP000003494};
RN   [1] {ECO:0000313|EMBL:EEP27529.1, ECO:0000313|Proteomes:UP000003494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14600 {ECO:0000313|EMBL:EEP27529.1,
RC   ECO:0000313|Proteomes:UP000003494};
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., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:EEP27529.1}.
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DR   EMBL; ACIP02000007; EEP27529.1; -; Genomic_DNA.
DR   RefSeq; WP_006907200.1; NZ_GG665867.1.
DR   AlphaFoldDB; C4GDQ0; -.
DR   STRING; 626523.GCWU000342_02224; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_6_1_9; -.
DR   Proteomes; UP000003494; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR10066; BETA-GLUCURONIDASE; 1.
DR   PANTHER; PTHR10066:SF67; BETA-GLUCURONIDASE; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEP27529.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003494}.
FT   DOMAIN          13..187
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          293..609
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   617 AA;  70164 MW;  E3BFCFBB65380DE3 CRC64;
     MLYPIMTPSR LVEDLAGIWD FQLDPEERGF AEKWYEKPLK DPMTMPVPAS FNDLKDGSDF
     RDYHGWVFYQ RRISLPAFMA KQRVMLRFDA ATHHANVYLN GRLIAEHQGG FLPFEVEITD
     DLREGEDNLL TVAINNFIDN TTLPVGMIGN MLGGNLGASP EPKHPGPNFD FFNYAGLNRT
     VRIYTTPGQY IADLTVTSQI DGEDGTRPIA DGKKALLNYT VAVGGQEDPA LARDAHVEVY
     DEEGNKVAEA NGLSGQLTIE QARLWRPLNA YLYRIRVSYG EDIYELPYGI RTVKVVGNRF
     LINGRKFYFK GYGKHEDTFP HGRGINLAMN TRDISIMKWQ GANSFRTSHY PYSEEMMRQC
     DREGIVVIDE TTAVGINYLF GGGANFGGKK VGTFDPEHGV KTQEHHREVI RDLIARDKNH
     ACVVLWSIAN EPDSSGQGAY EYFKPLFDLA RELDPQKRPV TLVSVQMAGG PDTDVSAQLS
     DVICLNRYYG WYFGAPDLEW SAQQMRAEMD QWEKLGKPLV FTEFGADTVM GMHDTTPVMY
     TEEYQLDYYK MNLAVMDDYP CVTGEQVWNF ADFATSQSIL RIQGNKKGLF TRDRKPKLAA
     HFFRDRWHAV PDFDYKD
//
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