ID   PYRB_SALAI              Reviewed;         308 AA.
AC   A8LY14;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Sare_1846;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000850; ABV97731.1; -; Genomic_DNA.
DR   RefSeq; WP_012182036.1; NC_009953.1.
DR   AlphaFoldDB; A8LY14; -.
DR   SMR; A8LY14; -.
DR   STRING; 391037.Sare_1846; -.
DR   PRIDE; A8LY14; -.
DR   EnsemblBacteria; ABV97731; ABV97731; Sare_1846.
DR   GeneID; 5704709; -.
DR   KEGG; saq:Sare_1846; -.
DR   PATRIC; fig|391037.6.peg.1874; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_11; -.
DR   OMA; FPTEREY; -.
DR   OrthoDB; 1844275at2; -.
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   3: Inferred from homology;
KW   Pyrimidine biosynthesis; Transferase.
FT   CHAIN           1..308
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000334591"
SQ   SEQUENCE   308 AA;  33007 MW;  BF3284B98256B0FA CRC64;
     MIRHLLSGAD VDAGTANRIL DTAAEMATVA GREVKKLPAL RGRTVVNLFY EDSTRTRISF
     EAAAKRLSAD VINFSAKGSS VTKGESLKDT ALTLQAMGAD AVVVRHPASG APHRLAEWVD
     GSVVNAGDGT HEHPTQALLD AYTMRSRLGR LAGLSVAVVG DVLHSRVARS NVLLLSTLGA
     KVTLVGPPPL IPVDIVAALA PGTAVCYDLD AVLPQSDVVM MLRVQRERMN DSYFPSAREY
     ARRYGLDGTR MRRLPEHAIV MHPGPMNRGM EITPEVADSP RSTIVEQVAN GVSVRMAVLY
     LLLGGNNR