ID   PYRB_BORPE              Reviewed;         317 AA.
AC   Q7W044;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   28-JAN-2026, entry version 113.
DE   RecName: Full=Aspartate carbamoyltransferase catalytic subunit {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=BP0321;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes the condensation of carbamoyl phosphate and
CC       aspartate to form carbamoyl aspartate and inorganic phosphate, the
CC       committed step in the de novo pyrimidine nucleotide biosynthesis
CC       pathway. {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate +
CC         phosphate + H(+); 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   -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC       organized as two trimers (C3), and six regulatory PyrI chains organized
CC       as three dimers (R2). {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
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DR   EMBL; BX640411; CAE40698.1; -; Genomic_DNA.
DR   RefSeq; WP_003820560.1; NC_002929.2.
DR   AlphaFoldDB; Q7W044; -.
DR   SMR; Q7W044; -.
DR   STRING; 257313.BP0321; -.
DR   PaxDb; 257313-BP0321; -.
DR   GeneID; 69603427; -.
DR   KEGG; bpe:BP0321; -.
DR   PATRIC; fig|257313.5.peg.347; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_4; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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-UniRule.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   FunFam; 3.40.50.1370:FF:000007; Aspartate carbamoyltransferase; 1.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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   NCBIfam; TIGR00670; asp_carb_tr; 1.
DR   NCBIfam; NF002032; PRK00856.1; 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.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..317
FT                   /note="Aspartate carbamoyltransferase catalytic subunit"
FT                   /id="PRO_0000113106"
FT   BINDING         65
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         66
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         93
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         115
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         145
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         148
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         178
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         233
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         274
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT   BINDING         275
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
SQ   SEQUENCE   317 AA;  34362 MW;  464A99C633295756 CRC64;
     MLNPQLNRHG ELIHLLSTEG LPRRIIEQIL DLAATFVPAP GQEFPKLPLL HGKSVFNLFF
     ENSTRTRTTF EIAAKRLSAD VVNLNIAASS TSKGESLLDT IANLSAMQAD LFVVRHGASG
     APYLIAQHVA PHVHVINAGD GRHAHPTQAL LDMYTIRHHK GDFNQLTVAI VGDVLHSRVA
     RSDIHALTTL GVPEVRVVAP ATLLPEGLAQ MGVRVCTDME EGLRDADVVI MLRLQNERMR
     GALLPSAHEY FKHYGLTQAR LALARPDAIV MHPGPMNRGV EIASEVADSG QAVILDQVTF
     GIAVRMAAMS LVAGVRP
//