RUTD_PSE14
ID RUTD_PSE14 Reviewed; 259 AA.
AC Q48MQ7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=PSPPH_1045;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ35275.1; -; Genomic_DNA.
DR RefSeq; WP_011167872.1; NC_005773.3.
DR AlphaFoldDB; Q48MQ7; -.
DR SMR; Q48MQ7; -.
DR STRING; 264730.PSPPH_1045; -.
DR ESTHER; pse14-q48mq7; RutD.
DR EnsemblBacteria; AAZ35275; AAZ35275; PSPPH_1045.
DR KEGG; psp:PSPPH_1045; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_50_1_6; -.
DR OMA; HAMSVTD; -.
DR OrthoDB; 1196738at2; -.
DR Proteomes; UP000000551; Chromosome.
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; IPR022742; Hydrolase_4.
DR InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR Pfam; PF12146; Hydrolase_4; 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..259
FT /note="Putative carbamate hydrolase RutD"
FT /id="PRO_0000402978"
SQ SEQUENCE 259 AA; 28540 MW; A6457622099B4EA4 CRC64;
MFHEIHRCQH ADAPLLVLSS GLGGSSRYWA DDLAALTRDH DVLVYDHAGT GRSPADLPAD
YSIRHMAMEL LTLLDSLGIQ RCHFMGHALG GLVGLEIALL RPELLQSQVL INAWSSPNPH
SARCFSVRKK LLLNSGPDAY VQAQALFLYP ADWIAANGAR LADDEAHALA HFPGTDNLLR
RIHALQTFDV EASLARIQTP TLLIANRDDM LVPWQQSQHL AEALPNARLV LLEYGGHASN
ITDPLPFQRT LLDFLNAQT