ID   RUTC_PANAM              Reviewed;         128 AA.
AC   D4GEU6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=PANA_4035;
OS   Pantoea ananatis (strain LMG 20103).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=706191;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20103;
RX   PubMed=20348253; DOI=10.1128/jb.00060-10;
RA   De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA   Coutinho T.A.;
RT   "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT   Eucalyptus blight and dieback.";
RL   J. Bacteriol. 192:2936-2937(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; CP001875; ADD79202.1; -; Genomic_DNA.
DR   RefSeq; WP_013027868.1; NC_013956.2.
DR   AlphaFoldDB; D4GEU6; -.
DR   SMR; D4GEU6; -.
DR   STRING; 706191.PANA_4035; -.
DR   EnsemblBacteria; ADD79202; ADD79202; PANA_4035.
DR   GeneID; 57270381; -.
DR   KEGG; pam:PANA_4035; -.
DR   eggNOG; COG0251; Bacteria.
DR   HOGENOM; CLU_100715_7_3_6; -.
DR   OMA; MPKTIIT; -.
DR   OrthoDB; 1850770at2; -.
DR   BioCyc; PANA706191:PANA_RS20505-MON; -.
DR   Proteomes; UP000001702; 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   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..128
FT                   /note="3-aminoacrylate deaminase RutC"
FT                   /id="PRO_0000402760"
SQ   SEQUENCE   128 AA;  13556 MW;  8E5ADAC0C321BA34 CRC64;
     MPKRAIIPAG SGVPLAPFVP GTLADGVLYV SGTLPFDKDN NVVHVGDAAA QTRHVLEIIK
     SVIETAGGSM DDVTMNSIFI TDWANYGAVN QVYAEYFPGE KPARFCIQCG LVKPDALIEI
     ASIAHLGK