ID   PYRX_PSEPU              Reviewed;         424 AA.
AC   Q59712;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Dihydroorotase-like protein;
DE   AltName: Full=Aspartate carbamoyltransferase 44 kDa non-catalytic chain;
GN   Name=pyrC' {ECO:0000303|PubMed:7896697};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC   STRAIN=PPN-1;
RX   PubMed=7896697; DOI=10.1128/jb.177.7.1751-1759.1995;
RA   Schurr M.J., Vickrey J.F., Kumar A.P., Campbell A.L., Cunin R.,
RA   Benjamin R.C., Shanley M.S., O'Donovan G.A.;
RT   "Aspartate transcarbamoylase genes of Pseudomonas putida: requirement for
RT   an inactive dihydroorotase for assembly into the dodecameric holoenzyme.";
RL   J. Bacteriol. 177:1751-1759(1995).
CC   -!- FUNCTION: Non-functional DHOase. {ECO:0000305|PubMed:7896697}.
CC   -!- SUBUNIT: Heterododecamer of 6 active PyrB subunits and 6 non-catalytic
CC       PyrC' subunits. {ECO:0000269|PubMed:7896697}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. PyrC' subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M97254; AAA69779.1; -; Genomic_DNA.
DR   PIR; B56144; B56144.
DR   AlphaFoldDB; Q59712; -.
DR   SMR; Q59712; -.
DR   STRING; 1240350.AMZE01000005_gene2534; -.
DR   eggNOG; COG0044; Bacteria.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd01317; DHOase_IIa; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   Pyrimidine biosynthesis.
FT   CHAIN           1..424
FT                   /note="Dihydroorotase-like protein"
FT                   /id="PRO_0000147286"
SQ   SEQUENCE   424 AA;  44265 MW;  87159A625340AC7C CRC64;
     MTISILGARV IDPKTGLDQV TDLHLDGGRI AAIGAAPAGF SASRTIQADG VVAAPGLVDL
     GVSLREPGYS RKGNIRSETR AAVAGGVTSL CCPPQTRPVL DTLAVAELIL DRAREAANSK
     VYPIGALTKG LEGEQLAELV ALRDTGCVAF GNGLKQIPNN RTLARALEYA ATFDLTVVFH
     SQDRDLAEGG LAHEGAMASF LGLPGIPESA ETVALARNLL LVEQSGVRAH FSQITSARGA
     QLIAQAQELG LPVTADVALY QLILTDESVR QFSSLYHVQP PLRTAKDRDG LRAAVKSGVI
     QAISSHHQPH ERDAKLAPFG ATEPGISSVE LLLPLAMTLV QDGLLDLPTL LARLSSGPAA
     ALRVPAGELK VGGAADLVLF DPQASTVAGE QWSSRGENCP FIGHCLPGAV RYTLVDGHVC
     HGPE