ID   PYRI_SALTY              Reviewed;         153 AA.
AC   P08421;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN   Name=pyrI; OrderedLocusNames=STM4459;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=3036524; DOI=10.1111/j.1432-1033.1987.tb13483.x;
RA   Michaels G., Kelln R.A., Nargang F.E.;
RT   "Cloning, nucleotide sequence and expression of the pyrBI operon of
RT   Salmonella typhimurium LT2.";
RL   Eur. J. Biochem. 166:55-61(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Involved in allosteric regulation of aspartate
CC       carbamoyltransferase.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
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 PyrI family. {ECO:0000305}.
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DR   EMBL; X05641; CAA29130.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL23278.1; -; Genomic_DNA.
DR   PIR; S00050; DTEBCT.
DR   RefSeq; NP_463319.1; NC_003197.2.
DR   RefSeq; WP_000148570.1; NC_003197.2.
DR   AlphaFoldDB; P08421; -.
DR   SMR; P08421; -.
DR   STRING; 99287.STM4459; -.
DR   PaxDb; P08421; -.
DR   EnsemblBacteria; AAL23278; AAL23278; STM4459.
DR   GeneID; 1255985; -.
DR   KEGG; stm:STM4459; -.
DR   PATRIC; fig|99287.12.peg.4692; -.
DR   HOGENOM; CLU_128576_0_0_6; -.
DR   OMA; CPNRNCI; -.
DR   PhylomeDB; P08421; -.
DR   BioCyc; SENT99287:STM4459-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.140; -; 1.
DR   HAMAP; MF_00002; Asp_carb_tr_reg; 1.
DR   InterPro; IPR020545; Asp_carbamoyltransf_reg_N.
DR   InterPro; IPR002801; Asp_carbamoylTrfase_reg.
DR   InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR   InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR   InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR   PANTHER; PTHR35805; PTHR35805; 1.
DR   Pfam; PF01948; PyrI; 1.
DR   Pfam; PF02748; PyrI_C; 1.
DR   SUPFAM; SSF54893; SSF54893; 1.
DR   SUPFAM; SSF57825; SSF57825; 1.
DR   TIGRFAMs; TIGR00240; ATCase_reg; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Pyrimidine biosynthesis; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..153
FT                   /note="Aspartate carbamoyltransferase regulatory chain"
FT                   /id="PRO_0000142314"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   153 AA;  17087 MW;  5C5730A07D45FD6F CRC64;
     MTHDNKLQVE AIKCGTVIDH IPAQVGFKLL SLFKLTETDQ RITIGLNLPS GEMGRKDLIK
     IENTFLTEEQ VNQLALYAPQ ATVNRIDNYD VVGKSRPSLP ERINNVLVCP NSNCISHAEP
     VSSSFAVKKR ANDIALKCKY CEKEFSHYVV LAN