ID PYRI_NATPD Reviewed; 153 AA.
AC Q3IPU7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002};
GN Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; OrderedLocusNames=NP_3520A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49851.1; -; Genomic_DNA.
DR RefSeq; WP_011323471.1; NC_007426.1.
DR AlphaFoldDB; Q3IPU7; -.
DR SMR; Q3IPU7; -.
DR STRING; 348780.NP_3520A; -.
DR EnsemblBacteria; CAI49851; CAI49851; NP_3520A.
DR GeneID; 3703088; -.
DR KEGG; nph:NP_3520A; -.
DR eggNOG; arCOG04229; Archaea.
DR HOGENOM; CLU_128576_0_0_2; -.
DR OrthoDB; 7000at2157; -.
DR Proteomes; UP000002698; 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; Reference proteome; Zinc.
FT CHAIN 1..153
FT /note="Aspartate carbamoyltransferase regulatory chain"
FT /id="PRO_0000321508"
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 135
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"
SQ SEQUENCE 153 AA; 16439 MW; 0E3A48E3BEFB26F9 CRC64;
MTDTELRVSK IQKGTVIDHI AGGQALNVLA ILGIDGTSGD EISVGMNVPS DRLGRKDIVK
VEGRELSQNE VDVLSLIAPA ATINIVRDFE VIEKHRVTRP ETVEGVLSCP NANCITTENE
PVDSRFEVLE AGVRCSYCGT IIRESLAAHI SVA
//
