RUTC_PSEU2
ID RUTC_PSEU2 Reviewed; 127 AA.
AC Q4ZXR9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Psyr_0997;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY36053.1; -; Genomic_DNA.
DR RefSeq; WP_003408714.1; NC_007005.1.
DR RefSeq; YP_234091.1; NC_007005.1.
DR AlphaFoldDB; Q4ZXR9; -.
DR SMR; Q4ZXR9; -.
DR STRING; 205918.Psyr_0997; -.
DR EnsemblBacteria; AAY36053; AAY36053; Psyr_0997.
DR KEGG; psb:Psyr_0997; -.
DR PATRIC; fig|205918.7.peg.1026; -.
DR eggNOG; COG0251; Bacteria.
DR HOGENOM; CLU_100715_7_3_6; -.
DR OMA; MPKTIIT; -.
DR Proteomes; UP000000426; 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..127
FT /note="3-aminoacrylate deaminase RutC"
FT /id="PRO_0000402763"
SQ SEQUENCE 127 AA; 13627 MW; 155871EF801AD2DA CRC64;
MTKKAIIPAG TSKPIAPFVP GSMADGVLYV SGTLPFDKDN NVVHVGDATA QTRHVLEAIK
SVVETAGGTL DDVTFNMIMI RDWADYAKVN EVYAEYFAGE KPARYCIQCG LVKPEALIEI
ASIAHIG