ID   A7ZLE4_ECO24            Unreviewed;       755 AA.
AC   A7ZLE4;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 84.
DE   SubName: Full=Glycosyl hydrolase, family 65 {ECO:0000313|EMBL:ABV17590.1};
GN   OrderedLocusNames=EcE24377A_1527 {ECO:0000313|EMBL:ABV17590.1};
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV17590.1, ECO:0000313|Proteomes:UP000001122};
RN   [1] {ECO:0000313|Proteomes:UP000001122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC       {ECO:0000256|ARBA:ARBA00006768}.
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DR   EMBL; CP000800; ABV17590.1; -; Genomic_DNA.
DR   RefSeq; WP_000198061.1; NC_009801.1.
DR   AlphaFoldDB; A7ZLE4; -.
DR   KEGG; ecw:EcE24377A_1527; -.
DR   HOGENOM; CLU_006285_2_1_6; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:TreeGrafter.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR037018; GH65_N.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000313|EMBL:ABV17590.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001122};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..277
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          298..660
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   DOMAIN          672..728
FT                   /note="Glycoside hydrolase family 65 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03633"
FT   ACT_SITE        473
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT   BINDING         333..334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT   BINDING         573..574
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ   SEQUENCE   755 AA;  84803 MW;  613CCEFE7741E185 CRC64;
     MTRPVTLSEP HFSQHTLNKY ASLMAQGNGY LGLRASHEED YTSQTRGMYL AGLYHRAGKG
     EINELVNLPD ILGMEIAING EVFSLSREAW QRELDFASGE LRRSVVWRTS NGTGYTIASR
     RFVSADQLPL IVLEITITPL DADASVLIST GIDATQTNHG RQHLDETQVR VFGQHLMQGI
     YTTQDGRSDV AISCCCMVSG DVQQCYTAKE RRLQQHTSAQ LHAGETVTLQ KLVWIDWRDD
     RQAVLDEWGS ASLRQLEMCA QQSYDQLLAV STENWRQWWQ KRRITVNGGE AHDQQALDYA
     LYHLRIMTPA HDERSSIAAK GLTGEGYKGH VFWDTEVFLL PFHLFSDPTV ARSLLRYRWH
     NLPGAQEKAR RNGWQGALFP WESARSGEEE TPEFAAINIR TGLRQKVASA QAEHHLVADI
     AWAVIQYWQT TGDESFIAHE GMALLLETAK FWISRAVRVN DRLEIHDVIG PDEYTEHVNN
     NAFTSYMAYY NVQQALSIAR QFGCSDDAFI HRAEMFLKEL RLPEIQPDGV LPQDDSFMAK
     PAINLAKYKA AAGKQTILLD YSRAEVNEMQ ILKQADVVML NYMLPEQFSA ASCLANLQFY
     EPRTIHDSSL SKAIHGIVAA RCGLLTQSYQ FWREGTEIDL GADPHSCDDG IHAAATGAIW
     LGAIQGFAGV SVRDGELHLN PALPEQWQQL SFPLFWQGCE LQVTLDAQRI AIRTSAPVSL
     RLNGQLISVA EESVFCLGDF ILPFNGTATT HQEDE
//