ID   RUTC_CAUSK              Reviewed;         129 AA.
AC   B0SW61;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=Caul_3980;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K31;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000927; ABZ73105.1; -; Genomic_DNA.
DR   RefSeq; WP_012287996.1; NC_010338.1.
DR   AlphaFoldDB; B0SW61; -.
DR   SMR; B0SW61; -.
DR   STRING; 366602.Caul_3980; -.
DR   EnsemblBacteria; ABZ73105; ABZ73105; Caul_3980.
DR   KEGG; cak:Caul_3980; -.
DR   eggNOG; COG0251; Bacteria.
DR   HOGENOM; CLU_100715_7_3_5; -.
DR   OMA; MPKTIIT; -.
DR   OrthoDB; 1850770at2; -.
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_0000402716"
SQ   SEQUENCE   129 AA;  13849 MW;  C1EF0D9F3AB41D00 CRC64;
     MPKTVIIPPG TGTPIAPFSP GTLADGIVYV SGTLAFDKDN NVANPDDAEA QTRQVLETIK
     SVIETAGGTM DDVTMNHIFL TDWSNYQTIN KVYAEYFPGD KPARYCIQCG LVKPGFVVEI
     ASVAHIGKT