ID   PYRB_IGNH4              Reviewed;         305 AA.
AC   A8A8H6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=Igni_0044;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N., Wall M.A.,
RA   Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W., Deciu C.,
RA   Hutchison D., Eads J.R., Anderson A., Fernandes F., Szeto E., Lapidus A.,
RA   Kyrpides N.C., Saier M.H. Jr., Richardson P.M., Rachel R., Huber H.,
RA   Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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}.
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DR   EMBL; CP000816; ABU81228.1; -; Genomic_DNA.
DR   RefSeq; WP_011998080.1; NC_009776.1.
DR   AlphaFoldDB; A8A8H6; -.
DR   SMR; A8A8H6; -.
DR   STRING; 453591.Igni_0044; -.
DR   EnsemblBacteria; ABU81228; ABU81228; Igni_0044.
DR   GeneID; 5562632; -.
DR   KEGG; iho:Igni_0044; -.
DR   eggNOG; arCOG00911; Archaea.
DR   HOGENOM; CLU_043846_1_2_2; -.
DR   OMA; FPTEREY; -.
DR   OrthoDB; 51351at2157; -.
DR   PhylomeDB; A8A8H6; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000000262; 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..305
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_1000000009"
SQ   SEQUENCE   305 AA;  34345 MW;  68C8BD90E38C93AF CRC64;
     MPDVVDVLDL DKKDMIKIFE LAEDIEYKKL HKSKWCALEN KTVSLLFVEP STRTRLSFEE
     SAKRLCAHTL TIVGEEASSF VKGESLYDTI KVLDKISDII VIRHNLDGSA KYASEVAANP
     VINAGDGKNQ HPTQSLIDLY VVRKRKGGLE DLRYAVVGDL RYARTARSFL LALTKFKPRS
     VYLVAPEVLK PSIKFLEELK SMGLNVFEVD RLEDVIPNVD VIYVTRIQKE RFPDPSEYEK
     VKGSYKITLD LIKRGKGDLI VLHPLPRVDE LDVRIDSTPH AAYFDQVAAS VPVRMATLAW
     SAGVV