ID   PYRI_PYRAB              Reviewed;         152 AA.
AC   P77919; G8ZHD1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN   Name=pyrI; OrderedLocusNames=PYRAB13260; ORFNames=PAB1499;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=9209027; DOI=10.1128/jb.179.13.4143-4157.1997;
RA   Purcarea C., Herve G., Ladjimi M.M., Cunin R.;
RT   "Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon
RT   Pyrococcus abyssi: genetic organization, structure, and expression in
RT   Escherichia coli.";
RL   J. Bacteriol. 179:4143-4157(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; U61765; AAB62985.1; -; Genomic_DNA.
DR   EMBL; AJ248287; CAB50231.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70768.1; -; Genomic_DNA.
DR   PIR; B75042; B75042.
DR   RefSeq; WP_010868441.1; NC_000868.1.
DR   AlphaFoldDB; P77919; -.
DR   SMR; P77919; -.
DR   STRING; 272844.PAB1499; -.
DR   GeneID; 1496714; -.
DR   KEGG; pab:PAB1499; -.
DR   PATRIC; fig|272844.11.peg.1411; -.
DR   eggNOG; arCOG04229; Archaea.
DR   HOGENOM; CLU_128576_0_0_2; -.
DR   OrthoDB; 7000at2157; -.
DR   PhylomeDB; P77919; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; 2.30.30.20; Aspartate carbamoyltransferase regulatory subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.70.140; Aspartate carbamoyltransferase regulatory subunit, N-terminal domain; 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   NCBIfam; TIGR00240; ATCase_reg; 1.
DR   PANTHER; PTHR35805; ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR35805:SF1; ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN; 1.
DR   Pfam; PF01948; PyrI; 1.
DR   Pfam; PF02748; PyrI_C; 1.
DR   SUPFAM; SSF57825; Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain; 1.
DR   SUPFAM; SSF54893; Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Pyrimidine biosynthesis; Zinc.
FT   CHAIN           1..152
FT                   /note="Aspartate carbamoyltransferase regulatory chain"
FT                   /id="PRO_0000142337"
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         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  16958 MW;  05DEE2DD0839A384 CRC64;
     MAELKVSAIK EGTVIDHIPA GKGLKVIEIL KLGKLTNGGA VLLAMNVPSK KLGRKDIVKV
     EGRFLSEEEV NKIALVAPNA TVNIIRDYKV VEKFKVEVPD VIEGILRCGN PNCITNHEYV
     TTKFYVISRE PLKVRCHYCE RTMEEEEILA NL
//