ID   PYRB_BACCL              Reviewed;         308 AA.
AC   P41008;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Aspartate carbamoyltransferase;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB;
OS   Bacillus caldolyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 405 / NBRC 15313 / YP-T;
RX   PubMed=7516791; DOI=10.1099/00221287-140-3-479;
RA   Ghim S.Y., Nielsen P., Neuhard J.;
RT   "Molecular characterization of pyrimidine biosynthesis genes from the
RT   thermophile Bacillus caldolyticus.";
RL   Microbiology 140:479-491(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RC   STRAIN=DSM 405 / NBRC 15313 / YP-T;
RX   PubMed=8206848; DOI=10.1128/jb.176.12.3698-3707.1994;
RA   Ghim S.Y., Neuhard J.;
RT   "The pyrimidine biosynthesis operon of the thermophile Bacillus
RT   caldolyticus includes genes for uracil phosphoribosyltransferase and uracil
RT   permease.";
RL   J. Bacteriol. 176:3698-3707(1994).
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;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; X73308; CAA51736.1; -; Genomic_DNA.
DR   EMBL; X76083; CAA53698.1; -; Genomic_DNA.
DR   PIR; I40166; I40166.
DR   AlphaFoldDB; P41008; -.
DR   SMR; P41008; -.
DR   PRIDE; P41008; -.
DR   UniPathway; UPA00070; UER00116.
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..308
FT                   /note="Aspartate carbamoyltransferase"
FT                   /id="PRO_0000113091"
SQ   SEQUENCE   308 AA;  34871 MW;  FAAA34EA1620291A CRC64;
     MTHLFALSEL PLDEIHRLLD EAERFRSGRI WRPAAPMYVA NLFFEPSTRT KCSFEMAERK
     LGLHVIPFDP ERSSVQKGET LYDTVRTLEA IGVDAVVIRH HEDAYFEALR HAVGIPIINA
     GDGCGHHPTQ SLLDLLTIRQ EFGAFTGLTV AIIGDIRHSR VARSNAEVLT RLGANVLFSG
     PEEWKDETNP YGTYVEVDEA IARADVVMLL RIQHERHAET MGLTKEEYHA RYGLTLERAR
     RMKSGAIILH PAPVNRGVEI ASELVEAKAS RIFKQMENGV YVRMAVLKRA MEGRMEHGRM
     AEKWHVVQ