YGEW_ECOLI
ID YGEW_ECOLI Reviewed; 396 AA.
AC Q46803; Q2M9X0; Q6BF62;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Putative carbamoyltransferase YgeW {ECO:0000305};
DE EC=2.1.3.- {ECO:0000305|PubMed:21557323};
DE AltName: Full=UTCase {ECO:0000303|PubMed:21557323};
GN Name=ygeW; OrderedLocusNames=b2870, JW5463;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4] {ECO:0007744|PDB:3Q98}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), PRELIMINARY FUNCTION, SUBUNIT, AND
RP DOMAIN.
RX PubMed=21557323; DOI=10.1002/prot.23043;
RA Li Y., Jin Z., Yu X., Allewell N.M., Tuchman M., Shi D.;
RT "The ygeW encoded protein from Escherichia coli is a knotted ancestral
RT catabolic transcarbamylase.";
RL Proteins 79:2327-2334(2011).
CC -!- FUNCTION: Putative carbamoyltransferase. No activity can be detected
CC with allantoin or 25 other related compounds, including 20 naturally
CC occurring amino acids, N-acetyl-L-ornithine, N-succinyl-L-ornithine, L-
CC ornithine, oxamate, beta-alanine and putrescine.
CC {ECO:0000269|PubMed:21557323}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:21557323}.
CC -!- DOMAIN: Contains a carbamoyl phosphate domain (CPD) and a second
CC substrate domain (SSD), which are linked by two helices.
CC {ECO:0000269|PubMed:21557323}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83051.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U28375; AAA83051.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48152.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76936.1; -; Genomic_DNA.
DR PIR; F65070; F65070.
DR RefSeq; WP_000978544.1; NZ_SSTT01000003.1.
DR RefSeq; YP_026185.1; NC_000913.3.
DR PDB; 3Q98; X-ray; 2.00 A; A=1-396.
DR PDBsum; 3Q98; -.
DR AlphaFoldDB; Q46803; -.
DR SMR; Q46803; -.
DR BioGRID; 4261510; 19.
DR STRING; 511145.b2870; -.
DR jPOST; Q46803; -.
DR PaxDb; Q46803; -.
DR PRIDE; Q46803; -.
DR EnsemblBacteria; AAT48152; AAT48152; b2870.
DR EnsemblBacteria; BAE76936; BAE76936; BAE76936.
DR GeneID; 945826; -.
DR KEGG; ecj:JW5463; -.
DR KEGG; eco:b2870; -.
DR PATRIC; fig|511145.12.peg.2963; -.
DR EchoBASE; EB2865; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_3_6; -.
DR InParanoid; Q46803; -.
DR OMA; IDHPTQA; -.
DR PhylomeDB; Q46803; -.
DR BioCyc; EcoCyc:G7489-MON; -.
DR EvolutionaryTrace; Q46803; -.
DR PRO; PR:Q46803; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Putative carbamoyltransferase YgeW"
FT /id="PRO_0000113263"
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"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 32..50
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 234..247
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:3Q98"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 314..318
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:3Q98"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:3Q98"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:3Q98"
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
