ID   PYRB_VIBC3              Reviewed;         309 AA.
AC   A5F5C9; C3M4Z9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 76.
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};
GN   OrderedLocusNames=VC0395_A2092, VC395_2624;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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=ABQ21919.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ACP10610.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000627; ABQ21919.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001235; ACP10610.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000013845.1; NZ_JAACZH010000021.1.
DR   AlphaFoldDB; A5F5C9; -.
DR   SMR; A5F5C9; -.
DR   STRING; 345073.VC395_2624; -.
DR   EnsemblBacteria; ABQ21919; ABQ21919; VC0395_A2092.
DR   KEGG; vco:VC0395_A2092; -.
DR   KEGG; vcr:VC395_2624; -.
DR   PATRIC; fig|345073.21.peg.2526; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_1_2_6; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000000249; Chromosome 2.
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; Transferase.
FT   CHAIN           1..309
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000321181"
SQ   SEQUENCE   309 AA;  34350 MW;  AD073EE793872BA5 CRC64;
     MANSLYQKHI ISIAELSRAE LELIVKTAGQ LKAQPNPELI KHKVVASCFF EPSTRTRLSF
     ETAIQRIGGS VIGFDNGGNT SLAKKGETLA DSVRVISSYV DAFVMRHPQE GAARLASEFS
     NGIPVINAGD GSNQHPSQTL LDLYSIFETQ GRLDNLDVAF VGDLKYGRTV HSLAQALAKF
     DNNRFYFVAP EALAMPDYIC EELDEAGVKY QVFSDMESVI PELDILYMTR VQKERFDESE
     YAHIKSAYIL TAAHLSDARS NLKVLHPLPR VDEITTDVDK TPHAYYFEQV ENGVYAREAL
     LALVLNESL