RUTC_METRJ
ID RUTC_METRJ Reviewed; 128 AA.
AC B1M5I6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-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};
GN OrderedLocusNames=Mrad2831_1582;
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 / 0-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-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; CP001001; ACB23577.1; -; Genomic_DNA.
DR RefSeq; WP_012318565.1; NC_010505.1.
DR AlphaFoldDB; B1M5I6; -.
DR SMR; B1M5I6; -.
DR STRING; 426355.Mrad2831_1582; -.
DR EnsemblBacteria; ACB23577; ACB23577; Mrad2831_1582.
DR KEGG; mrd:Mrad2831_1582; -.
DR eggNOG; COG0251; Bacteria.
DR HOGENOM; CLU_100715_7_3_5; -.
DR OMA; MPKTIIT; -.
DR OrthoDB; 1850770at2; -.
DR Proteomes; UP000006589; 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..128
FT /note="3-aminoacrylate deaminase RutC"
FT /id="PRO_0000402759"
SQ SEQUENCE 128 AA; 13499 MW; C726C16EB99B856E CRC64;
MPKQVVIPPG TGKPLAPYVP GTLADGVLYV SGTLPLDAEA NVVHVGDAAA QTRHVLETIK
GVVEAAGGTM DDVTFNHVFL ADWADYAAIN AVYAEYFPGE KPARYCIQCG LVKPEARVEI
AAIAHIGR