ID   PYRI_VIBPA              Reviewed;         153 AA.
AC   Q87LF7;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002};
GN   Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; OrderedLocusNames=VP2655;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: Involved in allosteric regulation of aspartate
CC       carbamoyltransferase. {ECO:0000255|HAMAP-Rule:MF_00002}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00002};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00002};
CC   -!- SUBUNIT: Contains catalytic and regulatory chains. {ECO:0000255|HAMAP-
CC       Rule:MF_00002}.
CC   -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00002}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000031; BAC60918.1; -; Genomic_DNA.
DR   RefSeq; NP_799034.1; NC_004603.1.
DR   RefSeq; WP_005455107.1; NC_004603.1.
DR   AlphaFoldDB; Q87LF7; -.
DR   SMR; Q87LF7; -.
DR   STRING; 223926.28807665; -.
DR   EnsemblBacteria; BAC60918; BAC60918; BAC60918.
DR   GeneID; 1190200; -.
DR   KEGG; vpa:VP2655; -.
DR   PATRIC; fig|223926.6.peg.2550; -.
DR   eggNOG; COG1781; Bacteria.
DR   HOGENOM; CLU_128576_0_0_6; -.
DR   OMA; NNVFECP; -.
DR   Proteomes; UP000002493; Chromosome 1.
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   CHAIN           1..153
FT                   /note="Aspartate carbamoyltransferase regulatory chain"
FT                   /id="PRO_0000142319"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
SQ   SEQUENCE   153 AA;  17405 MW;  564A373E1E187FD3 CRC64;
     MAKETQLQVE AIKNGTVIDH IPAQIGIKVL KLFDMHNSSQ RVTIGLNLPS SALGHKDLLK
     IENVFINEEQ ASKLALYAPH ATVNQIENYE VVKKLALELP EKINNVFECP NSNCISHNEP
     VESSFKVFEK KEEIRLKCKY CEKVFSREIV TER