ID   RUTC_CAUVN              Reviewed;         129 AA.
AC   B8H1Q2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=CCNA_02886;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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}.
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DR   EMBL; CP001340; ACL96351.1; -; Genomic_DNA.
DR   RefSeq; WP_010920637.1; NC_011916.1.
DR   RefSeq; YP_002518259.1; NC_011916.1.
DR   AlphaFoldDB; B8H1Q2; -.
DR   SMR; B8H1Q2; -.
DR   EnsemblBacteria; ACL96351; ACL96351; CCNA_02886.
DR   GeneID; 7331316; -.
DR   KEGG; ccs:CCNA_02886; -.
DR   PATRIC; fig|565050.3.peg.2816; -.
DR   HOGENOM; CLU_100715_7_3_5; -.
DR   OMA; MPKTIIT; -.
DR   OrthoDB; 1850770at2; -.
DR   PhylomeDB; B8H1Q2; -.
DR   Proteomes; UP000001364; 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; Reference proteome.
FT   CHAIN           1..129
FT                   /note="3-aminoacrylate deaminase RutC"
FT                   /id="PRO_0000402714"
SQ   SEQUENCE   129 AA;  13889 MW;  5B544CA64AFB328D CRC64;
     MPKTVITPPG TQTPIAPFSP GTLADGIVYV SGTLAFDKDN NVAFPGDAEA QTRQVLETIK
     SVIETAGGTM EDVTMNHIFL TDWVHYAPMN KVYAEYFPGD KPARYCIQCG LVKPGFVVEI
     ASVAHIGKT