ID L0G059_ECHVK Unreviewed; 820 AA.
AC L0G059;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Beta-galactosidase/beta-glucuronidase {ECO:0000313|EMBL:AGA79544.1};
GN OrderedLocusNames=Echvi_3321 {ECO:0000313|EMBL:AGA79544.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA79544.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-2012) 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; CP003346; AGA79544.1; -; Genomic_DNA.
DR RefSeq; WP_015267089.1; NC_019904.1.
DR AlphaFoldDB; L0G059; -.
DR STRING; 926556.Echvi_3321; -.
DR KEGG; evi:Echvi_3321; -.
DR PATRIC; fig|926556.3.peg.3502; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_0_2_10; -.
DR OMA; YLYRSIW; -.
DR OrthoDB; 811652at2; -.
DR Proteomes; UP000010796; Chromosome.
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; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048229; GalB-like.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
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; NF041463; GalB; 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; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000010796};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..820
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003942856"
FT DOMAIN 32..199
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 209..309
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 314..477
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 637..702
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 715..814
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 820 AA; 93161 MW; 4A3C2C79757F02E5 CRC64;
MRFRSILICL LLIGSICSFS HAQRVRKSWP LKEDWRFSKG EQEEAYQIDF DDREWESVQV
PHDWAIYGPF DESNDLQIVA VTQNGEKVAT KKTGRTGGLP YMGVGWYRRA FEVPGFDPEK
QRVKLIFDGA MSEAQVYVNG EKVGFWPYGY NSFYFDVTDF LHADGTKNQL AVRLENKPQS
SRWYPGAGLY RNVHVLVTPK IHVPVWGTFV TTPYVSEEYA SVNIKTELEH VSEGTDISIE
TSILDLSGKV VAKKKNVQRL NHGRPLEQFL TVDHPELWSP ESPHLYVAKS VISIEGREID
EFTTRFGIRK IEFIADKGFF LNGQRRKFQG VNLHHDLGPL GAAVNRSAIK RQLQLMKDMG
ADAIRTSHNM PAPELVELCD EMGLMVMVES FDEWDVAKCK NGYHRFFDDW AEKDLVNMVR
HYRNHPSVVM WSIGNEVPTQ CSADGYQVAK FLQDICHRED PTRLVTAGMD QISCVLDNGF
AAMIDVTGFN YRTHRYEEGY QKLPHSLVLG SETGSTVSSR GVYHFPVEKG AQVIHENQQS
SAYGLEYCSW SNLPEDDFAL ADDFDWTLGQ FVWTGFDYLG EPTPYDTDAW PNHSSMFGIV
DLAGIPKDRY YLYKSVWKPE EETLHILPHW NWEGREGQKT PLFVYTNYPS AELFINGESQ
GKQTKHKEGT LQERYRLMWM DAIYEPGEVK VVAYDSLGKK AAEKILHTAG KPHHIELVPE
NKRIAVEGDE LAFIRVQVVD KEGRVCPTDQ RSLSFDVAGA GAFRAVANGD PGSLELFHEP
QMKVFNGQLT LIVSAKEAGN IHIKATAKGL KNGETIMEAY
//