ID   PYRI_VIBS2              Reviewed;         153 AA.
AC   P96175;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN   Name=pyrI;
OS   Vibrio sp. (strain 2693).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=79682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9611817; DOI=10.1099/00221287-144-5-1435;
RA   Xu Y., Zhang Y., Liang Z., Van de Casteele M., Legrain C., Glansdorff N.;
RT   "Aspartate carbamoyltransferase from a psychrophilic deep-sea bacterium,
RT   Vibrio strain 2693: properties of the enzyme, genetic organization and
RT   synthesis in Escherichia coli.";
RL   Microbiology 144:1435-1441(1998).
CC   -!- FUNCTION: Involved in allosteric regulation of aspartate
CC       carbamoyltransferase. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Contains catalytic and regulatory chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000305}.
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DR   EMBL; Y09786; CAA70924.1; -; Genomic_DNA.
DR   PIR; T48883; T48883.
DR   AlphaFoldDB; P96175; -.
DR   SMR; P96175; -.
DR   EvolutionaryTrace; P96175; -.
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   CHAIN           1..153
FT                   /note="Aspartate carbamoyltransferase regulatory chain"
FT                   /id="PRO_0000142320"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   153 AA;  16870 MW;  BA0FDCA23CE60378 CRC64;
     MKSNHMQVEA ICNGYVIDHI PSGQGVKILR LFSLTDTKQR VTVGFNLPSH DGTTKDLIKV
     ENTEITKSQA NQLALLAPNA TVNIIENFKV TDKHSLALPK EVENVFPCPN SNCITHGEPV
     ISSFTIKMIK GNIGLKCKYC EKTFSKEIVT AQV