PYRB_THET8
ID PYRB_THET8 Reviewed; 302 AA.
AC Q5SK66;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=TTHA0782;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; AP008226; BAD70605.1; -; Genomic_DNA.
DR RefSeq; WP_011172874.1; NC_006461.1.
DR RefSeq; YP_144048.1; NC_006461.1.
DR AlphaFoldDB; Q5SK66; -.
DR SMR; Q5SK66; -.
DR STRING; 300852.55772164; -.
DR EnsemblBacteria; BAD70605; BAD70605; BAD70605.
DR GeneID; 3169148; -.
DR KEGG; ttj:TTHA0782; -.
DR PATRIC; fig|300852.9.peg.775; -.
DR eggNOG; COG0540; Bacteria.
DR HOGENOM; CLU_043846_2_0_0; -.
DR OMA; FPTEREY; -.
DR PhylomeDB; Q5SK66; -.
DR BRENDA; 2.1.3.2; 2305.
DR UniPathway; UPA00070; UER00116.
DR Proteomes; UP000000532; 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..302
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113221"
SQ SEQUENCE 302 AA; 33015 MW; 630EFD0E2237B709 CRC64;
MRHLLDFQGW SRTEVESLLD TARVMREVLE RPIKKVPALQ GFTVATVFFE PSTRTRISFE
LAARRMSADV VSFAAQTSSL QKGESYKDTL LTLEAMGVDA YVIRADSAGV PHQATRWVKG
AVINGGDGRR AHPTQALLDA YTLLEALGTL EGKKVAIVGD ILHSRVARSG AELLSLLGAQ
VFCAGPPSLL PQSLPGAHLT PRLEEALEEA DAVMVLRLQK ERMEAGLVHL EDYVARYQVT
EKRLALAKPQ APLLHPGPMN RDVELEGTLA DSARSLVNRQ VQNGVAVRMA VLYHLLVGRE
KA