ID   PYRI_NITMS              Reviewed;         153 AA.
AC   A9A2Q6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002};
GN   Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; OrderedLocusNames=Nmar_1687;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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}.
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DR   EMBL; CP000866; ABX13583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A2Q6; -.
DR   SMR; A9A2Q6; -.
DR   STRING; 436308.Nmar_1687; -.
DR   PRIDE; A9A2Q6; -.
DR   EnsemblBacteria; ABX13583; ABX13583; Nmar_1687.
DR   KEGG; nmr:Nmar_1687; -.
DR   eggNOG; arCOG04229; Archaea.
DR   HOGENOM; CLU_128576_0_0_2; -.
DR   OMA; CPNRNCI; -.
DR   PhylomeDB; A9A2Q6; -.
DR   Proteomes; UP000000792; 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; 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_1000088830"
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;  17433 MW;  9883E4A184F449B5 CRC64;
     MEQSELMVRR IKEGTVIDHI DEGKGIQVLN ALRIDGSDGS LITIALNVPS GKFKKKDIIK
     VENKFLKDDD TNKLAVIAPK ATINMIKDYK LVEKRRVSLP NEIDRIFRCS NPDCVTNSTE
     HIESIMDVID KEGRVLKCRY CSRVLDVNQL KYN