ID   PYRB_PSYT1              Reviewed;         332 AA.
AC   Q934T0;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB;
OS   Psychrobacter sp. (strain TAD1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=81861;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sun K., Hommais F., Bertin P., Pothier J., Di Prisco G., Danchin A.,
RA   Herve G.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=9682487; DOI=10.1111/j.1574-6968.1998.tb13112.x;
RA   Sun K., Camardella L., Di Prisco G., Herve G.;
RT   "Properties of aspartate transcarbamylase from TAD1, a psychrophilic
RT   bacterial strain isolated from Antarctica.";
RL   FEMS Microbiol. Lett. 164:375-382(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   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; AJ416110; CAD01098.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q934T0; -.
DR   SMR; Q934T0; -.
DR   UniPathway; UPA00070; UER00116.
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   1: Evidence at protein level;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..332
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113181"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  36248 MW;  54B80EB31309586C CRC64;
     MPNTHDTKNN VSPSEYAKFD PSTIHQRLNT SLSRPQLNSD GSIRHFLGVE GLNKAQLQAI
     IAKALFFEPS TRTRTTFEVA EKRLGANVLN LDIASSSAKK GESLRDTLWN LQAMTADIFV
     VRHSASGAAH FMATEVTPDI AIINGGDGWH AHPTQGMLDM LTIHREAPRP FEELSVAIIG
     DVKHSRVARS DISALQTLGV KDIRVIAPRT LLPKGIERFG VQVYEDMNSC VRDCDVIMGL
     RIQNERIGSP LLASSSEYYK QYGITPERVA LAKPDALIMH PGPMNRGVEI ASSVADGPQS
     VILKQVSNGV AIRMAVLALT MEGQRAHQAN RG