ID   PYRI_SERMA              Reviewed;         154 AA.
AC   P19936;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN   Name=pyrI;
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   -!- 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; J05033; AAA26565.1; -; Genomic_DNA.
DR   PIR; C34396; DTSECM.
DR   AlphaFoldDB; P19936; -.
DR   SMR; P19936; -.
DR   STRING; 273526.SMDB11_4605; -.
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; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..154
FT                   /note="Aspartate carbamoyltransferase regulatory chain"
FT                   /id="PRO_0000142315"
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   154 AA;  17306 MW;  2947AFC4362140FD CRC64;
     MTHDNKLQVE AIKCGTVIDH IPAQIGFKLL TLFKLTATDQ RITIGLNLPS NELGRKDLIK
     IENTFLTEQQ ANQLAMYAPK ATVNRIDNYE VVRKLTLSLP DHIDGVLTCP NGNCISRSEP
     VRSSFSVKSR GGEVHLKCRY CEKEFEHQVV LQAD