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
//