ID   PYRI_BIFLO              Reviewed;         139 AA.
AC   Q8G656;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN   Name=pyrI; OrderedLocusNames=BL0793;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24608.1; -; Genomic_DNA.
DR   RefSeq; NP_695972.1; NC_004307.2.
DR   RefSeq; WP_007052224.1; NC_004307.2.
DR   AlphaFoldDB; Q8G656; -.
DR   SMR; Q8G656; -.
DR   STRING; 206672.BL0793; -.
DR   EnsemblBacteria; AAN24608; AAN24608; BL0793.
DR   GeneID; 66505153; -.
DR   KEGG; blo:BL0793; -.
DR   PATRIC; fig|206672.9.peg.494; -.
DR   HOGENOM; CLU_128576_0_0_11; -.
DR   OMA; CPNRNCI; -.
DR   PhylomeDB; Q8G656; -.
DR   Proteomes; UP000000439; 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-KW.
DR   Gene3D; 3.30.70.140; -; 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.
PE   3: Inferred from homology;
KW   Metal-binding; Pyrimidine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..139
FT                   /note="Aspartate carbamoyltransferase regulatory chain"
FT                   /id="PRO_0000142297"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  15518 MW;  E437B575872CE477 CRC64;
     MEVTSIQNGI IIDHVPAGTS LKVLEYLKID PAKTKLALIM NADSKRYGSK DIIKIEDDKD
     IDLDVLGFVA RQATVDVVRG GKIVEKKQPN LPEHIVGVIS CVNPRCVTTA EPGIKQMFHL
     VHSERLEYRC DYCDEEAKL