ID   PYRB_PSEPU              Reviewed;         334 AA.
AC   Q59711;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SUBUNIT: Heterododecamer of 6 active PyrB subunits and 6 non-catalytic
CC       PyrC' subunits.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; M97253; AAD15279.1; -; Genomic_DNA.
DR   PIR; A56144; A56144.
DR   RefSeq; WP_016501977.1; NZ_UGUX01000003.1.
DR   AlphaFoldDB; Q59711; -.
DR   SMR; Q59711; -.
DR   STRING; 1240350.AMZE01000005_gene2535; -.
DR   GeneID; 45526542; -.
DR   eggNOG; COG0540; Bacteria.
DR   UniPathway; UPA00070; UER00116.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..334
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113178"
SQ   SEQUENCE   334 AA;  36410 MW;  6226A3AC1EAB3960 CRC64;
     MTPIDAKRPL QLNDQGQLRH FLSLDGLPRE LLTEILDTAD SFLEVGARAV KKVPLLRGKT
     VCNVFFENST RTRTTFELAA QRLSADVISL NVSTSSTSKG ETLFDTLRNL EAMAADMFVV
     RHSDSGAAHF IAEHVCPDVA VINGGDGRHA HPTQGMLDML TIRRHKGSFE NLSVAIVGDI
     LHSRVARSDM LALKALGCPD IRVIGPKTLI PIGIEQYGVK VYTDLAEGLK DVDVVIMLRL
     QRERMAGGLL PSEGEFYRLF GLTTARLACA KPDAIVMHPG PINRGVEIES AVADGKHSVI
     LNQVTYGIAV RMAVLSMAMS GQNAQRQFDQ ENAQ