ID   PYRB_VIBVY              Reviewed;         309 AA.
AC   Q7MHF1;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 117.
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=VV2920;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(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}.
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DR   EMBL; BA000037; BAC95684.1; -; Genomic_DNA.
DR   RefSeq; WP_011151229.1; NC_005139.1.
DR   AlphaFoldDB; Q7MHF1; -.
DR   SMR; Q7MHF1; -.
DR   STRING; 672.VV93_v1c26430; -.
DR   EnsemblBacteria; BAC95684; BAC95684; BAC95684.
DR   KEGG; vvy:VV2920; -.
DR   PATRIC; fig|196600.6.peg.2901; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_1_2_6; -.
DR   OMA; GDGPNEH; -.
DR   OrthoDB; 1844275at2; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000002675; Chromosome I.
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..309
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113227"
SQ   SEQUENCE   309 AA;  34266 MW;  B7AE74490C0BE969 CRC64;
     MTNSLYKKHI ISIPELSRAE LELIVKTAGQ LKAEPNPELI KNKVVASCFF EPSTRTRLSF
     ETAIQRIGGD VIGFDDGGNT SLAKKGETLS DSVQVISNYV DAFVMRHPQE GAARLASEFS
     NGVPVINAGD GANQHPTQTL LDLFTISETQ DRLDNLNVAF VGDLKYGRTV HSLTQALAKF
     NNIRFFFVAP DALAMPDYIL EDLDEAGISY SLHTDMETVI PELDILYMTR VQKERFDESE
     YAHIKSAYIL TAALLEGARE NLKVLHPLPR VDEITTDVDK TPHAYYFQQA GNGVYAREAL
     LALVLNESL