ID   PYRB_HALSA              Reviewed;         310 AA.
AC   Q9HHN4;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   25-MAY-2022, entry version 110.
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=VNG_6309G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OG   Plasmid pNRC200.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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   -!- SUBUNIT: Heterooligomer of catalytic and regulatory chains.
CC       {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG20942.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004438; AAG20942.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_012289640.1; NZ_BK010831.1.
DR   AlphaFoldDB; Q9HHN4; -.
DR   SMR; Q9HHN4; -.
DR   EnsemblBacteria; AAG20942; AAG20942; VNG_6309G.
DR   GeneID; 5954945; -.
DR   GeneID; 62888210; -.
DR   KEGG; hal:VNG_6309G; -.
DR   PATRIC; fig|64091.14.peg.2288; -.
DR   HOGENOM; CLU_043846_1_2_2; -.
DR   InParanoid; Q9HHN4; -.
DR   OrthoDB; 51351at2157; -.
DR   PhylomeDB; Q9HHN4; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000000554; Plasmid pNRC200.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
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   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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   Plasmid; Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..310
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113245"
SQ   SEQUENCE   310 AA;  34396 MW;  CFBFB4CEBD52749D CRC64;
     MDLDHIITSK QLSRADIETV LDRAAEIDAD PSAFADRYEN TVLGLLFFEP STRTKMSFDT
     AMKRLGGDIV DMGSVDSSSV KKGETLADTV RVIEGYADAL VLRHPNQGAA QMASEFVDVP
     LLNAGDGAGH HPTQTLLDLY TIRENAGLED LTIGIMGDLK YGRTVHSLSR ALTNFDVDQH
     FISPESLQLP RDVVYDLEQE SGTRVREHDS FEDVLPELDI LYVTRIQRER FPDENEYQKV
     AGEYQLTATH LEAAKDDLTI MHPLPRVDEI APEIDDTDHA AYFEQAHNGV PVRMALLDLV
     LSADGGVDDE