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Database: UniProt
Entry: C4L212_EXISA
LinkDB: C4L212_EXISA
Original site: C4L212_EXISA 
ID   C4L212_EXISA            Unreviewed;       478 AA.
AC   C4L212;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   SubName: Full=Glycoside hydrolase family 1 {ECO:0000313|EMBL:ACQ69186.1};
GN   OrderedLocusNames=EAT1b_0253 {ECO:0000313|EMBL:ACQ69186.1};
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ69186.1, ECO:0000313|Proteomes:UP000000716};
RN   [1] {ECO:0000313|EMBL:ACQ69186.1, ECO:0000313|Proteomes:UP000000716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX   PubMed=21460088; DOI=10.1128/JB.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC       {ECO:0000256|ARBA:ARBA00010838, ECO:0000256|RuleBase:RU003690}.
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DR   EMBL; CP001615; ACQ69186.1; -; Genomic_DNA.
DR   RefSeq; WP_012726305.1; NC_012673.1.
DR   AlphaFoldDB; C4L212; -.
DR   STRING; 360911.EAT1b_0253; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   KEGG; eat:EAT1b_0253; -.
DR   eggNOG; COG2723; Bacteria.
DR   HOGENOM; CLU_001859_0_2_9; -.
DR   OMA; NPLFLWT; -.
DR   OrthoDB; 9765195at2; -.
DR   Proteomes; UP000000716; 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; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353:SF85; ARYL-PHOSPHO-BETA-D-GLUCOSIDASE BGLA; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU004468};
KW   Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:ACQ69186.1}.
FT   ACT_SITE        377
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   478 AA;  54607 MW;  B1CFD53A6CAB65CB CRC64;
     MKTLPKDFLW GGALAAHQFE GGWDADGKGP SVVDVLTAGA HGVARRITDK VEPNEFYPNH
     EAIDFYHRYK EDVALFAEMG LKCLRTSIGW SRIFPNGDDA EPNEAGLQFY DDLFDELLKY
     DIEPIITLSH FEMPLHLARE YGGFRNRAVV DHFVRFAEVC FDRYRDKVKY WMTFNEINNK
     MDVNNPLFLW TNSGVLLEEG ENAREVMYQT GHHELIASAL AVAKGKAINP DFEIGAMVSH
     VPIYPYSSNP DDVMLSEEMM RQRYFFPDVQ VRGFYPSYAL NEFEREGYNI PILEGDEEIL
     QNGKVDYLGF SYYMSTTVKS DVVADNSGDI VNGGLPNGVE NPYIQSSDWG WAIDPVGLRY
     VLNRLYDRYQ IPLFIVENGF GAVDEIVDGK IHDAARIDYL KAHIEQLKQA VLYDGVDLIG
     YTPWGIIDIV SFTTGEMKKR YGMIYVDRDN EGNGSMERMK KDSFDWYKRV IATNGENL
//
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