RUTC_HALO1
ID RUTC_HALO1 Reviewed; 130 AA.
AC D0LI57;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=Hoch_3937;
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Nannocystineae; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2;
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(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; CP001804; ACY16436.1; -; Genomic_DNA.
DR RefSeq; WP_012829035.1; NC_013440.1.
DR AlphaFoldDB; D0LI57; -.
DR SMR; D0LI57; -.
DR STRING; 502025.Hoch_3937; -.
DR EnsemblBacteria; ACY16436; ACY16436; Hoch_3937.
DR KEGG; hoh:Hoch_3937; -.
DR eggNOG; COG0251; Bacteria.
DR HOGENOM; CLU_100715_7_3_7; -.
DR OMA; MPKTIIT; -.
DR OrthoDB; 1850770at2; -.
DR Proteomes; UP000001880; 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..130
FT /note="3-aminoacrylate deaminase RutC"
FT /id="PRO_0000402750"
SQ SEQUENCE 130 AA; 14032 MW; 19751120FDEC5A45 CRC64;
MPMKPINPSQ FPKPIAPYSA GAMADNVVYV SGTLALGEGG QVLHVGDAKA QTRHVLETIK
TTLEAAGGGM ADITFNHIFV KSWDDYKAIN EVYAEYFPGD KPARYCIQCG LVKPELLVEI
ASIAHLSPKE