RUTD_VARPS
ID RUTD_VARPS Reviewed; 266 AA.
AC C5CN82;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Putative carbamate hydrolase RutD {ECO:0000255|HAMAP-Rule:MF_00832};
DE EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_00832};
DE AltName: Full=Aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00832};
GN Name=rutD {ECO:0000255|HAMAP-Rule:MF_00832}; OrderedLocusNames=Vapar_4841;
OS Variovorax paradoxus (strain S110).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=543728;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S110;
RX PubMed=21183664; DOI=10.1128/jb.00925-10;
RA Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA Ovchinnikova G., Goodwin L., Han C.;
RT "Complete genome sequence of the metabolically versatile plant growth-
RT promoting endophyte, Variovorax paradoxus S110.";
RL J. Bacteriol. 193:1183-1190(2011).
CC -!- FUNCTION: Involved in pyrimidine catabolism. May facilitate the
CC hydrolysis of carbamate, a reaction that can also occur spontaneously.
CC {ECO:0000255|HAMAP-Rule:MF_00832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamate + 2 H(+) = CO2 + NH4(+); Xref=Rhea:RHEA:15649,
CC ChEBI:CHEBI:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938; Evidence={ECO:0000255|HAMAP-Rule:MF_00832};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD
CC family. {ECO:0000255|HAMAP-Rule:MF_00832}.
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DR EMBL; CP001635; ACS21445.1; -; Genomic_DNA.
DR RefSeq; WP_015867601.1; NC_012791.1.
DR AlphaFoldDB; C5CN82; -.
DR SMR; C5CN82; -.
DR STRING; 543728.Vapar_4841; -.
DR EnsemblBacteria; ACS21445; ACS21445; Vapar_4841.
DR GeneID; 45059075; -.
DR KEGG; vap:Vapar_4841; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_50_1_4; -.
DR OMA; HAMSVTD; -.
DR OrthoDB; 1196738at2; -.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00832; RutD; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR03611; RutD; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..266
FT /note="Putative carbamate hydrolase RutD"
FT /id="PRO_0000402986"
FT DOMAIN 15..128
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00832"
SQ SEQUENCE 266 AA; 28021 MW; 2BDDA5B3F6F8CA7C CRC64;
MPLHYEVHGP ADGEAVLLSS GLGGSAAFWQ PQLGALLEAG HRVIAYDQRG TGRSPAALDA
GYAIADMARD VVQILDATAT PRCHLVGHAL GGLVGLQLAL DEPARVASLV LVNAWSKPNA
HSARCFDARL ALLDACGPRA YVEAQPIFLY PAAWCAEHAQ RVADEVDHAF AHFPGEANMR
ARIGALRAFD IDARLGAITA PTLVAAAMDD ALVPWTCSQR LADGLKDVTL HFLPHGGHAH
SVTEAAVFNR SLLDFLARVS APGVPA