ID   YGEW_ECOL6              Reviewed;         396 AA.
AC   Q8FE91;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative carbamoyltransferase YgeW {ECO:0000250|UniProtKB:Q46803};
DE            EC=2.1.3.- {ECO:0000250|UniProtKB:Q46803};
GN   Name=ygeW; OrderedLocusNames=c3448;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN81893.1; -; Genomic_DNA.
DR   RefSeq; WP_000978544.1; NZ_CP051263.1.
DR   AlphaFoldDB; Q8FE91; -.
DR   SMR; Q8FE91; -.
DR   STRING; 199310.c3448; -.
DR   PRIDE; Q8FE91; -.
DR   EnsemblBacteria; AAN81893; AAN81893; c3448.
DR   KEGG; ecc:c3448; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_3_6; -.
DR   OMA; IDHPTQA; -.
DR   BioCyc; ECOL199310:C3448-MON; -.
DR   Proteomes; UP000001410; 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   Transferase.
FT   CHAIN           1..396
FT                   /note="Putative carbamoyltransferase YgeW"
FT                   /id="PRO_0000113264"
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;  44187 MW;  62C5A199BB31FD46 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 SWAPYKVMEE RTELLRANDH EGLKALEKQC
     LAQNAQHKDW HCTEEMMELT RDGEALYMHC LPADISGVSC KEGEVTEGVF EKYRIATYKE
     ASWKPYIIAA MILSRKYAKP GALLEQLLKE AQERVK