ID   PYRB_PSEFA              Reviewed;         334 AA.
AC   P56585; Q9F4I6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB;
OS   Pseudomonas fluorescens biotype A.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=32035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCS365;
RA   Camacho-Carvajal M.M., Scheublin T., Lugtenberg B.J.J., Bloemberg G.V.;
RT   "The regulatory protein PyrR of Pseudomona fluorescens is required for
RT   competitive root colonization.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-19.
RC   STRAIN=ATCC 13525 / DSM 50090 / JCM 5963 / NBRC 14160 / NCIMB 9046 / NCTC
RC   10038 / VKM B-894;
RX   PubMed=8234318; DOI=10.1073/pnas.90.21.9818;
RA   Bergh S.T., Evans D.R.;
RT   "Subunit structure of a class A aspartate transcarbamoylase from
RT   Pseudomonas fluorescens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9818-9822(1993).
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; AY007523; AAG15558.1; -; Genomic_DNA.
DR   AlphaFoldDB; P56585; -.
DR   SMR; P56585; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..334
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113177"
FT   CONFLICT        6
FT                   /note="T -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="D -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  36463 MW;  18500AC9EBD1C659 CRC64;
     MTPLETKRPL QLNDQGQLQH FLSLDGLRRE LLTEILDTAD SFLEVGARAV KKVPLLRGKT
     VCNVFFENST RTRTTFELAA QRLSADVITL NVSTSSASKG ETLLDTLRNL EAMAADMFVV
     RHGDSGAAHF IAEHVCPQVA IINGGDGRHA HPTQGMLDML TIRRHKGSFE NLSVAIVGDI
     LHSRVARSNM LALKTLGCPD IRVIAPKTLL PIGVEQYGVK VYTDMTEGLK DVDVVIMLRL
     QRERMTGGLL PSEGEFYRLF GLTTARLAGA KPDAIVMHPG PINRGVEIES AVADGPHSVI
     LNQVTYGIAI RMAVLSMAMS GQTAQRQFDQ ENAQ