ID   RUTC_ECOL6              Reviewed;         128 AA.
AC   P0AFQ6; P75896;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=3-aminoacrylate deaminase RutC {ECO:0000255|HAMAP-Rule:MF_00831};
DE            Short=3-AA deaminase {ECO:0000255|HAMAP-Rule:MF_00831};
DE            EC=3.5.-.- {ECO:0000255|HAMAP-Rule:MF_00831};
GN   Name=rutC {ECO:0000255|HAMAP-Rule:MF_00831, ECO:0000303|PubMed:23143235};
GN   OrderedLocusNames=c1147;
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).
RN   [2] {ECO:0007744|PDB:3V4D}
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), SUBUNIT, AND DOMAIN.
RX   PubMed=23143235; DOI=10.1107/s1744309112041796;
RA   Knapik A.A., Petkowski J.J., Otwinowski Z., Cymborowski M.T., Cooper D.R.,
RA   Chruszcz M., Krajewska W.M., Minor W.;
RT   "Structure of Escherichia coli RutC, a member of the YjgF family and
RT   putative aminoacrylate peracid reductase of the rut operon.";
RL   Acta Crystallogr. F 68:1294-1299(2012).
CC   -!- FUNCTION: Involved in pyrimidine catabolism. Catalyzes the deamination
CC       of 3-aminoacrylate to malonic semialdehyde, a reaction that can also
CC       occur spontaneously. RutC may facilitate the reaction and modulate the
CC       metabolic fitness, rather than catalyzing essential functions.
CC       {ECO:0000255|HAMAP-Rule:MF_00831}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(Z)-3-aminoacrylate + H(+) + H2O = 3-oxopropanoate + NH4(+);
CC         Xref=Rhea:RHEA:34947, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:33190, ChEBI:CHEBI:59894;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00831};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00831,
CC       ECO:0000269|PubMed:23143235}.
CC   -!- DOMAIN: Contains a hydrophobic cavity in the center of the structure
CC       and ligand-binding clefts between two subunits.
CC       {ECO:0000269|PubMed:23143235}.
CC   -!- SIMILARITY: Belongs to the RutC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00831}.
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DR   EMBL; AE014075; AAN79615.1; -; Genomic_DNA.
DR   RefSeq; WP_001126780.1; NC_004431.1.
DR   PDB; 3V4D; X-ray; 1.95 A; A/B/C/D/E/F=1-128.
DR   PDBsum; 3V4D; -.
DR   AlphaFoldDB; P0AFQ6; -.
DR   SMR; P0AFQ6; -.
DR   STRING; 199310.c1147; -.
DR   EnsemblBacteria; AAN79615; AAN79615; c1147.
DR   GeneID; 66670712; -.
DR   KEGG; ecc:c1147; -.
DR   eggNOG; COG0251; Bacteria.
DR   HOGENOM; CLU_100715_7_3_6; -.
DR   OMA; MPKTIIT; -.
DR   BioCyc; ECOL199310:C1147-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.40; -; 1.
DR   HAMAP; MF_00831; RutC; 1.
DR   InterPro; IPR019897; RidA_CS.
DR   InterPro; IPR019898; RutC.
DR   InterPro; IPR035959; RutC-like_sf.
DR   InterPro; IPR006175; YjgF/YER057c/UK114.
DR   PANTHER; PTHR11803; PTHR11803; 1.
DR   Pfam; PF01042; Ribonuc_L-PSP; 1.
DR   SUPFAM; SSF55298; SSF55298; 1.
DR   TIGRFAMs; TIGR03610; RutC; 1.
DR   PROSITE; PS01094; UPF0076; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase.
FT   CHAIN           1..128
FT                   /note="3-aminoacrylate deaminase RutC"
FT                   /id="PRO_0000402382"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   STRAND          20..24
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   HELIX           48..65
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   STRAND          73..81
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   HELIX           86..96
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:3V4D"
FT   STRAND          118..125
FT                   /evidence="ECO:0007829|PDB:3V4D"
SQ   SEQUENCE   128 AA;  13763 MW;  7D5FC2374597D907 CRC64;
     MPKSVIIPAG SSAPLAPFVP GTLADGVVYV SGTLAFDQHN NVLFADDPKA QTRHVLETIR
     KVIETAGGTM ADVTFNSIFI TDWKNYAAIN EIYAEFFPGD KPARFCIQCG LVKPDALVEI
     ATIAHIAK