ID   PYRB_PSEAE              Reviewed;         334 AA.
AC   Q59653;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB; OrderedLocusNames=PA0402;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RA   Vickrey J.F., Schurr M.J., Benjamin R.C., Cunin R., Shanley M.S.,
RA   O'Donovan G.A.;
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; L19649; AAA25976.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG03791.1; -; Genomic_DNA.
DR   PIR; H83595; H83595.
DR   RefSeq; NP_249093.1; NC_002516.2.
DR   RefSeq; WP_003084569.1; NZ_QZGE01000016.1.
DR   AlphaFoldDB; Q59653; -.
DR   SMR; Q59653; -.
DR   STRING; 287.DR97_3370; -.
DR   PaxDb; Q59653; -.
DR   PRIDE; Q59653; -.
DR   DNASU; 878267; -.
DR   EnsemblBacteria; AAG03791; AAG03791; PA0402.
DR   GeneID; 878267; -.
DR   KEGG; pae:PA0402; -.
DR   PATRIC; fig|208964.12.peg.423; -.
DR   PseudoCAP; PA0402; -.
DR   HOGENOM; CLU_043846_2_0_6; -.
DR   InParanoid; Q59653; -.
DR   OMA; FPTEREY; -.
DR   PhylomeDB; Q59653; -.
DR   BioCyc; PAER208964:G1FZ6-406-MON; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
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   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT   CHAIN           1..334
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113176"
FT   CONFLICT        206
FT                   /note="R -> A (in Ref. 1; AAA25976)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  36629 MW;  2DC90450FA2E42E9 CRC64;
     MPTDAKRPLQ LNDQGQLRHF ISLDGLPREL LTEILDTADS FLEVGARAVK KVPLLRGKTV
     CNVFFENSTR TRTTFELAAQ RLSADVISLN VSTSSTSKGE TLTDTLRNLE AMAADMFVVR
     HSDSGAAHFI AEHVSPNVAV INGGDGRHAH PTQGMLDMLT IRRHKGNFEQ LSVAIVGDIL
     HSRVARSNML ALKTLGCPDI RVIAPRTLLP IGLEEQYGVR VFTNADEGLK DVDVVIMLRL
     QRERMQGGLL PSEGEFFKLY GLTEKRLKLA KPDAIVMHPG PINRGVEIES AVADGAQSVI
     LNQVTYGIAI RMAVLSMAMS GQNTQRQLEQ EDAE