ID   N9DRL1_9GAMM            Unreviewed;       265 AA.
AC   N9DRL1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Pyrimidine utilization protein D {ECO:0000313|EMBL:ENV83315.1};
GN   ORFNames=F941_01126 {ECO:0000313|EMBL:ENV83315.1};
OS   Acinetobacter bouvetii DSM 14964 = CIP 107468.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1120925 {ECO:0000313|EMBL:ENV83315.1, ECO:0000313|Proteomes:UP000018460};
RN   [1] {ECO:0000313|EMBL:ENV83315.1, ECO:0000313|Proteomes:UP000018460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 107468 {ECO:0000313|EMBL:ENV83315.1,
RC   ECO:0000313|Proteomes:UP000018460};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter bouvetii CIP 107468.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:ENV83315.1}.
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DR   EMBL; APQD01000009; ENV83315.1; -; Genomic_DNA.
DR   RefSeq; WP_005008789.1; NZ_KB892260.1.
DR   AlphaFoldDB; N9DRL1; -.
DR   PATRIC; fig|1120925.3.peg.1200; -.
DR   eggNOG; COG0596; Bacteria.
DR   OrthoDB; 9804723at2; -.
DR   Proteomes; UP000018460; 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:0006212; P:uracil catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          16..246
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   265 AA;  29667 MW;  BEB8C63FDD5E2259 CRC64;
     MHYQIHPCTD NAQAEHILLS SGLGGHGAFW KPQLEALQQH FHVLTYDHEG CHADAEALPA
     DYSMQHMAQQ ALSIIRDADI QQFHFIGHAL GGHIGMELAR LIAESRENLQ MKSLSCINAW
     DQLDLHTQKC FQARISLLKN SGAEAYVRAQ ALFLYPPQWI SEHQESLEQA ENAQLTSFPP
     AHNVLMRLQA LQQFSVNEQH AEALKNTQIQ LIANQDDFLV PVKKSADLQQ TLGLGELEIF
     ATGAHASTHT QTEKINQALL KFLLS
//