PYRB_BRUC2
ID PYRB_BRUC2 Reviewed; 322 AA.
AC A9MBN9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=BCAN_B0600;
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
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; CP000873; ABX63776.1; -; Genomic_DNA.
DR RefSeq; WP_004690217.1; NC_010104.1.
DR AlphaFoldDB; A9MBN9; -.
DR SMR; A9MBN9; -.
DR EnsemblBacteria; ABX63776; ABX63776; BCAN_B0600.
DR GeneID; 55592270; -.
DR KEGG; bcs:BCAN_B0600; -.
DR HOGENOM; CLU_043846_2_0_5; -.
DR OMA; FPTEREY; -.
DR PhylomeDB; A9MBN9; -.
DR UniPathway; UPA00070; UER00116.
DR PRO; PR:A9MBN9; -.
DR Proteomes; UP000001385; Chromosome II.
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..322
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_1000073721"
SQ SEQUENCE 322 AA; 34850 MW; 85DEF5016ADD7452 CRC64;
MTNQTVSPLF PHRHLLGIKG LSPLDILCLL DLAYQEIAVS RQPEKKKSVL RGRTQINLFF
EASTRTQSSF ELAGKRLGAD VMNMSVGNSS VKKGETLIDT AMTLNAMQPD ILVIRHASAG
AAALLAQKVG CSVVNAGDGA HEHPTQALLD ALTIRRAKGQ IENLIVAICG DVLHSRVARS
NILLLNALGA RVRVVAPSTL LPAGMADMSV EVFNSMEEGL KDADVVMMLR LQRERMAGSF
VPSVREYFHF YGLDREKLKF AKPDALVMHP GPMNRGVEIA SDVADGPQSV IQQQVEMGVA
VRMAVMEALL DPRRNPGNGE PA