ID   Q9UAH8_TRYCR            Unreviewed;       326 AA.
AC   Q9UAH8;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   13-SEP-2023, entry version 89.
DE   RecName: Full=aspartate carbamoyltransferase {ECO:0000256|ARBA:ARBA00013008};
DE            EC=2.1.3.2 {ECO:0000256|ARBA:ARBA00013008};
GN   Name=pyr2 {ECO:0000313|EMBL:BAA74525.1};
OS   Trypanosoma cruzi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=5693 {ECO:0000313|EMBL:BAA74525.1};
RN   [1] {ECO:0000313|EMBL:BAA74525.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tulahuen {ECO:0000313|EMBL:BAA74525.1};
RX   PubMed=9878395; DOI=10.1006/jmbi.1998.2293;
RA   Gao G., Nara T., Nakajima-Shimada J., Aoki T.;
RT   "Novel organization and sequences of five genes encoding all six enzymes
RT   for de novo pyrimidine biosynthesis in Trypanosoma cruzi.";
RL   J. Mol. Biol. 285:149-161(1999).
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         Evidence={ECO:0000256|ARBA:ARBA00001363};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004852}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. {ECO:0000256|RuleBase:RU003634}.
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DR   EMBL; AB017765; BAA74525.1; -; Genomic_DNA.
DR   PIR; T30522; T30522.
DR   AlphaFoldDB; Q9UAH8; -.
DR   VEuPathDB; TriTrypDB:C3747_31g124; -.
DR   VEuPathDB; TriTrypDB:C4B63_60g116; -.
DR   VEuPathDB; TriTrypDB:ECC02_000695; -.
DR   VEuPathDB; TriTrypDB:Tc_MARK_8869; -.
DR   VEuPathDB; TriTrypDB:TcBrA4_0007060; -.
DR   VEuPathDB; TriTrypDB:TcCL_ESM11130; -.
DR   VEuPathDB; TriTrypDB:TcCLB.508375.30; -.
DR   VEuPathDB; TriTrypDB:TcCLB.511643.30; -.
DR   VEuPathDB; TriTrypDB:TcG_08241; -.
DR   VEuPathDB; TriTrypDB:TCSYLVIO_001183; -.
DR   VEuPathDB; TriTrypDB:TcYC6_0066550; -.
DR   UniPathway; UPA00070; UER00116.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
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:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
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   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003634}.
FT   DOMAIN          13..153
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          160..323
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
SQ   SEQUENCE   326 AA;  35963 MW;  0A11066F181F612D CRC64;
     MLELPPVASL KGKSITSAEQ FSRADIYALI HLASAMQRKI DAGEVLNLLQ GRIMTPLFFE
     DSSRTFSSFC AAMIRLGGSV VNFKVEASSI NKGETLADTI RTLDSYSDVL VMRHPRQDAI
     EEALSVAQHP ILNAGNGAGE HPTQALLDTL TIHSELGSVD GITIALIGDL KMGRTVHSLL
     KLLVRNFSIK CVFLVAPDAL QMPQDVLEPL QHEIATKGVI IHRTHALTDE VMQKSDVLYT
     TRLQKERFMA STSDDAAALQ SFAAKTDITI DAARIRLAKE KMIVMHPLPR NDELSTTVDA
     DPRAAYFRQM RYGMFMRMAI LWSVLA
//