ID   V4NFK6_9CAUL            Unreviewed;       276 AA.
AC   V4NFK6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Putative carbamate hydrolase RutD {ECO:0000256|HAMAP-Rule:MF_00832};
DE            EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_00832};
DE   AltName: Full=Aminohydrolase {ECO:0000256|HAMAP-Rule:MF_00832};
GN   Name=rutD {ECO:0000256|HAMAP-Rule:MF_00832};
GN   ORFNames=AEYBE204_05005 {ECO:0000313|EMBL:ESQ80632.1};
OS   Asticcacaulis sp. YBE204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ80632.1, ECO:0000313|Proteomes:UP000017808};
RN   [1] {ECO:0000313|EMBL:ESQ80632.1, ECO:0000313|Proteomes:UP000017808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBE204 {ECO:0000313|EMBL:ESQ80632.1,
RC   ECO:0000313|Proteomes:UP000017808};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
CC   -!- FUNCTION: Involved in pyrimidine catabolism. May facilitate the
CC       hydrolysis of carbamate, a reaction that can also occur spontaneously.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00832};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD
CC       family. {ECO:0000256|HAMAP-Rule:MF_00832}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESQ80632.1}.
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DR   EMBL; AWGF01000002; ESQ80632.1; -; Genomic_DNA.
DR   RefSeq; WP_023461303.1; NZ_AWGF01000002.1.
DR   AlphaFoldDB; V4NFK6; -.
DR   STRING; 1282363.AEYBE204_05005; -.
DR   PATRIC; fig|1282363.3.peg.991; -.
DR   OrthoDB; 9801400at2; -.
DR   Proteomes; UP000017808; Unassembled WGS sequence.
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; alpha/beta hydrolase; 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   NCBIfam; TIGR03611; RutD; 1.
DR   PANTHER; PTHR43433:SF5; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43433; HYDROLASE, ALPHA/BETA FOLD FAMILY PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00832};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017808}.
FT   DOMAIN          32..134
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   276 AA;  30001 MW;  0963C842DE11278B CRC64;
     MLASEVKPFP EAETVTISGL AVKLYGRKAG IPVILSPGLG GHGAYWSPQV EALCEKFRVI
     LYDHRGTGGS DRDELSVSYH ARHMADDIAL ILEGLDYEAA HIVGHAAGAV AGLQLALDHP
     QKVLSLTCVN GWAVAEPHFK RCFEIRTAIY KSGGAEAYLK AQPLFLFPAE WINDHLEELD
     AQAAHHAPGF QSEANLLARI EALRDFDIRD RLEDITCPVM VIGTLDDMLV PVRSSAFLAE
     GLPNAQCRIV GWGGHAVNVT VPDEFNDILT TFLKGI
//