ID   YGEW_ECO57              Reviewed;         396 AA.
AC   Q8X6C0;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative carbamoyltransferase YgeW {ECO:0000250|UniProtKB:Q46803};
DE            EC=2.1.3.- {ECO:0000250|UniProtKB:Q46803};
GN   Name=ygeW; OrderedLocusNames=Z4209, ECs3743;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q46803}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. {ECO:0000305}.
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DR   EMBL; AE005174; AAG57999.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37166.1; -; Genomic_DNA.
DR   PIR; C85942; C85942.
DR   PIR; G91096; G91096.
DR   RefSeq; NP_311770.1; NC_002695.1.
DR   RefSeq; WP_000978553.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X6C0; -.
DR   SMR; Q8X6C0; -.
DR   STRING; 155864.EDL933_4071; -.
DR   EnsemblBacteria; AAG57999; AAG57999; Z4209.
DR   EnsemblBacteria; BAB37166; BAB37166; ECs_3743.
DR   GeneID; 916433; -.
DR   KEGG; ece:Z4209; -.
DR   KEGG; ecs:ECs_3743; -.
DR   PATRIC; fig|386585.9.peg.3905; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_3_6; -.
DR   OMA; IDHPTQA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR017702; Carbamoyltransferase_YgeW.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR03316; ygeW; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..396
FT                   /note="Putative carbamoyltransferase YgeW"
FT                   /id="PRO_0000113265"
FT   BINDING         71..74
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P04391"
FT   BINDING         98
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P04391"
FT   BINDING         165..168
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P04391"
FT   BINDING         330..331
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250|UniProtKB:P04391"
SQ   SEQUENCE   396 AA;  44186 MW;  C2C5B599B45C50F0 CRC64;
     MMKTVNELIK DINSLTSHLH EKDFLLTWEQ TPDELKQVLD VAAALKALRA ENISTKVFNS
     GLGISVFRDN STRTRFSYAS ALNLLGLAQQ DLDEGKSQIA HGETVRETAN MISFCADAIG
     IRDDMYLGAG NAYMREVGAA LDDGYKQGVL PQRPALVNLQ CDIDHPTQSM ADLAWLREHF
     GSLENLKGKK IAMTWAYSPS YGKPLSVPQG IIGLMTRFGM DVTLAHPEGY DLIPDVVEVA
     KNNAKASGGS FRQVTSMEEA FKDADIVYPK SWAPYKVMEQ RTELLRANDH EGLKALEKQC
     LAQNAQHKDW HCTEEMMELT RDGEALYMHC LPADISGVSC KEGEVTEGVF EKYRIATYKE
     ASWKPYIIAA MILSRKYAKP GALLEQLLKE AQERVK