ID   PYRB_VIBS2              Reviewed;         310 AA.
AC   P96174;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Aspartate carbamoyltransferase catalytic subunit;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB;
OS   Vibrio sp. (strain 2693).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=79682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9611817; DOI=10.1099/00221287-144-5-1435;
RA   Xu Y., Zhang Y., Liang Z., Van de Casteele M., Legrain C., Glansdorff N.;
RT   "Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium,
RT   Vibrio strain 2693: properties of the enzyme, genetic organization and
RT   synthesis in Escherichia coli.";
RL   Microbiology 144:1435-1441(1998).
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SUBUNIT: Contains six catalytic and six regulatory chains.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; Y09786; CAA70923.1; -; Genomic_DNA.
DR   PIR; T48882; T48882.
DR   AlphaFoldDB; P96174; -.
DR   SMR; P96174; -.
DR   PRIDE; P96174; -.
DR   UniPathway; UPA00070; UER00116.
DR   EvolutionaryTrace; P96174; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..310
FT                   /note="Aspartate carbamoyltransferase catalytic subunit"
FT                   /id="PRO_0000113228"
SQ   SEQUENCE   310 AA;  34419 MW;  10A3E593AC4ADAF9 CRC64;
     MANPLFRKHI VSINDISRNE LELIVKTAAK LKKQPQPELL KNKVIASCFF EASTRTRLSF
     ETAIQRLGGT VIGFDNASNT SLAKKGETLA DSISVISSYV DAFVMRHPQE GAARLASEFS
     NVPVINGGDG SNQHPTQTLL DLFSIYETQG CLDNLNIALV GDLKYGRTVH SLAQALAKFS
     GCKFYFIAPD ALAMPEYICD ELDEHNVSYA CYNSIEEVVP EIDVLYMTRV QKERFDETEY
     QHMKAGFILS ASSLKHAKDN LKVLHPLPRV DEIAVDVDKT PYAYYFQQAE NGVYAREALL
     ALVLNATIEG