ID J2GMP3_9SPHN Unreviewed; 260 AA.
AC J2GMP3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=PMI02_03909 {ECO:0000313|EMBL:EJL23988.1};
OS Novosphingobium sp. AP12.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1144305 {ECO:0000313|EMBL:EJL23988.1, ECO:0000313|Proteomes:UP000007515};
RN [1] {ECO:0000313|EMBL:EJL23988.1, ECO:0000313|Proteomes:UP000007515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP12 {ECO:0000313|EMBL:EJL23988.1,
RC ECO:0000313|Proteomes:UP000007515};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL23988.1}.
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DR EMBL; AKKE01000127; EJL23988.1; -; Genomic_DNA.
DR RefSeq; WP_007685599.1; NZ_AKKE01000127.1.
DR AlphaFoldDB; J2GMP3; -.
DR STRING; 1144305.PMI02_03909; -.
DR PATRIC; fig|1144305.3.peg.3671; -.
DR eggNOG; COG2267; Bacteria.
DR OrthoDB; 8680283at2; -.
DR Proteomes; UP000007515; 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:UP000007515}.
FT DOMAIN 18..129
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 260 AA; 27589 MW; B479FC9E98E9A04D CRC64;
MPEAGGLHHD FHGPEGAPTL ILSSGLGGAG GYWAPNLAAL SENHRVLTYD QRGTGRSDRA
LPETTSIADM AQDVVALMDA LDIDTAHFVG HALGGMIGIE ASLLSGRIDR LVVVNGWRTL
SPHTRRCFEA RLAILRGAGI EPFLRAQPLF LYPPDWIAAH DADLEAELAH HIAAFPGAET
MEKRIAAVAA WAPTSERLAK LRDVLVIATR DDFLVPQATS LDLAGPIPGA DIATFGWGGH
ACNVSDPKGF NRLALGFLGS
//
