ID   PYRB_COREF              Reviewed;         312 AA.
AC   Q8FT39;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Aspartate carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_00001};
DE            EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001};
DE   AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001};
DE            Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001};
GN   Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; OrderedLocusNames=CE1732;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00001};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-
CC       Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC18542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000035; BAC18542.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_006767732.1; NZ_GG700683.1.
DR   AlphaFoldDB; Q8FT39; -.
DR   SMR; Q8FT39; -.
DR   STRING; 196164.23493572; -.
DR   PRIDE; Q8FT39; -.
DR   EnsemblBacteria; BAC18542; BAC18542; BAC18542.
DR   KEGG; cef:CE1732; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_11; -.
DR   OMA; FPTEREY; -.
DR   OrthoDB; 1844275at2; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001409; Chromosome.
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; Reference proteome; Transferase.
FT   CHAIN           1..312
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113122"
SQ   SEQUENCE   312 AA;  33707 MW;  EEF40AAD98413D3B CRC64;
     MKHLLSIADL SRDEIISLLD EADRFKEVLE GREVKKLPTL RGRTIFTLFY ENSTRTRSSF
     ETAGKWMSAD VINISASSSS VKKGESLKDT GLTLSAIGAD AIIMRHPSSG AAQQLAGYVA
     PGGVGPSVIN AGDGSHQHPT QALLDALTLR QRLGGIEGRK IVIVGDILHS RVVRSNVDLL
     STLGAEVILV APPTLLPYGV ENWPVRTSYD MDAEIRDADA VMMLRVQQER MQGGFFPSHR
     EYATLYGMSK AREASLKDSA IIMHPGPMLR GMEINFGVAD APRTAVLQQV SNGVHVRMAV
     LFALVAGSDA TI