ID   PYRB_PROM0              Reviewed;         338 AA.
AC   A3PAV3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=P9301_02551;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000576; ABO16878.1; -; Genomic_DNA.
DR   RefSeq; WP_011862276.1; NC_009091.1.
DR   AlphaFoldDB; A3PAV3; -.
DR   SMR; A3PAV3; -.
DR   STRING; 167546.P9301_02551; -.
DR   EnsemblBacteria; ABO16878; ABO16878; P9301_02551.
DR   KEGG; pmg:P9301_02551; -.
DR   eggNOG; COG0540; Bacteria.
DR   HOGENOM; CLU_043846_2_0_3; -.
DR   OMA; FPTEREY; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000001430; Chromosome.
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..338
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000301602"
SQ   SEQUENCE   338 AA;  37390 MW;  D0DAFA93BB306940 CRC64;
     MQIWPHKHIH SLANFSIKDY ESVFELANRF DALKNSGTKK IPALQGTLVT SLFFEPSTRT
     KNSFELAAKR LSADVQTFAP SSSSLTKGET IIDTAITYSA MGADTLVIRH SSSYITFEIA
     EKLDAINSKT SVLNAGDGLH SHPSQGLLDI YTLIKFFSKN TLNPGVLNSK KILIIGDVNH
     SRVARSNLWA LSAFGADIIL CGPETLIPDE FTNFLKTPAP NQIEDPVKSR GCITISRSLE
     ESIKIADAII VLRLQKERMM ENLLSSIDSY SLDYGLTSEK LSLNNKEIPI LHPGPINRDI
     EISSKVVDQY PNCLINNQVS NGIPIRMALL YLLQKNNQ