ID   PYRB_BURP0              Reviewed;         343 AA.
AC   A3NYG2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 69.
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};
GN   OrderedLocusNames=BURPS1106A_3145;
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABN92549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000572; ABN92549.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004534003.1; NC_009076.1.
DR   AlphaFoldDB; A3NYG2; -.
DR   SMR; A3NYG2; -.
DR   EnsemblBacteria; ABN92549; ABN92549; BURPS1106A_3145.
DR   GeneID; 56594990; -.
DR   KEGG; bpl:BURPS1106A_3145; -.
DR   HOGENOM; CLU_043846_2_0_4; -.
DR   UniPathway; UPA00070; UER00116.
DR   Proteomes; UP000006738; Chromosome I.
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..343
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000329101"
SQ   SEQUENCE   343 AA;  37387 MW;  ADC079148CAAF53A CRC64;
     MTTDTSGRTG NPAAAAPAER FRYGFLKGNP QLTKNGELKH LLTIEGLPRA ILNQILDTAE
     QFVSVTDREV KKVPLLRGKS VFNLFFENST RTRTTFEIAA KRLSADVINL NINASSTSKG
     ESLLDTINNL SAMHADLFVV RHASSGAPYL IAEHCAPHVH VINAGDGRHA HPTQGLLDMY
     TIRHYKRDFT KLRVAIVGDI LHSRVARSDI HALTTLGVPE VRAIGPRTLL PGGLEQMGVR
     VFHNLDEGLR DVDVIIMLRL QNERMSGALL PSAQEYFKSW GLTPERLALA APDAIVMHPG
     PMNRGVEIDS QVADGPQSVI LNQVTFGIAV RMAVMGIVAG TSD