ID   PYRB_SERMA              Reviewed;         306 AA.
AC   P19910;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Aspartate carbamoyltransferase catalytic subunit;
DE            EC=2.1.3.2;
DE   AltName: Full=Aspartate transcarbamylase;
DE            Short=ATCase;
GN   Name=pyrB;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2674139; DOI=10.1016/s0021-9258(19)84752-x;
RA   Beck D., Kedzie K.M., Wild J.R.;
RT   "Comparison of the aspartate transcarbamoylases from Serratia marcescens
RT   and Escherichia coli.";
RL   J. Biol. Chem. 264:16629-16637(1989).
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: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC       organized as two trimers (C3), and six regulatory PyrI chains organized
CC       as three dimers (R2).
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. ATCase family. {ECO:0000305}.
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DR   EMBL; J05033; AAA26564.1; -; Genomic_DNA.
DR   PIR; B34396; OWSEAC.
DR   AlphaFoldDB; P19910; -.
DR   SMR; P19910; -.
DR   STRING; 273526.SMDB11_4606; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..306
FT                   /note="Aspartate carbamoyltransferase catalytic subunit"
FT                   /id="PRO_0000113190"
SQ   SEQUENCE   306 AA;  33371 MW;  2CBD163DC9480F33 CRC64;
     MANPLYHKHI ISINDLSRDD LELVLATAAG LKANPQPELL KHKVIASCFF EASTRTRLSF
     ETSMHRLGAS VVGFADGSNT SLGKKGETLA DTISVISTYV DAIVMRHPQE GARMASEFSG
     NVPVLNAGDG NQHPTQTLLD LFTIQETQGR LSNLSIAMVG DLKYGRTVHS LTQALAKFEG
     NRFYFIAPDA LAMPAYILKM LEEKGIEYSS HGSIEEVVPE LDILYMTRVQ KERLDPSEYA
     NVKAQFVLAA DLAGAANLKV LHPLPRIDEI ATDVDKTPHA YYFQQAGNGI FARSALALVV
     NADLAL