ID   RUTC_CAUST              Reviewed;         129 AA.
AC   D5VGV2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
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}; OrderedLocusNames=Cseg_2079;
OS   Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS   LMG 17158 / TK0059) (Mycoplana segnis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=509190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / TK0059;
RX   PubMed=21705585; DOI=10.1128/jb.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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   -!- SIMILARITY: Belongs to the RutC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00831}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002008; ADG10545.1; -; Genomic_DNA.
DR   RefSeq; WP_013079200.1; NC_014100.1.
DR   AlphaFoldDB; D5VGV2; -.
DR   SMR; D5VGV2; -.
DR   STRING; 509190.Cseg_2079; -.
DR   EnsemblBacteria; ADG10545; ADG10545; Cseg_2079.
DR   KEGG; cse:Cseg_2079; -.
DR   eggNOG; COG0251; Bacteria.
DR   HOGENOM; CLU_100715_7_3_5; -.
DR   OMA; MPKTIIT; -.
DR   OrthoDB; 1850770at2; -.
DR   Proteomes; UP000002629; 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; 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.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..129
FT                   /note="3-aminoacrylate deaminase RutC"
FT                   /id="PRO_0000402715"
SQ   SEQUENCE   129 AA;  13812 MW;  2F944EB24AF5D118 CRC64;
     MPKTVITPPG TGTPIAPFSP GTLADGIVYV SGTLAFDKDN NVAFPGDAEA QTRQVLETIK
     SVIETAGGTM EDVVMNHIFL TDWVHYAPMN KVYAEYFPGD KPARYCIQCG LVKPGFVVEI
     ASVAHIGKP