PYRI_SULAC
ID PYRI_SULAC Reviewed; 164 AA.
AC P74766; Q4J8H2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN Name=pyrI; OrderedLocusNames=Saci_1595;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RA Durbecq V., Thia-Toong T.-L., Roovers M., Legrain C., Glansdorff N.,
RA Charlier D.R.M.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=12142413; DOI=10.1128/jb.184.16.4430-4441.2002;
RA Thia-Toong T.-L., Roovers M., Durbecq V., Gigot D., Glansdorff N.,
RA Charlier D.R.M.;
RT "Genes of de novo pyrimidine biosynthesis from the hyperthermoacidophilic
RT crenarchaeote Sulfolobus acidocaldarius: novel organization in a bipolar
RT operon.";
RL J. Bacteriol. 184:4430-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; Y08309; CAA69618.1; -; Genomic_DNA.
DR EMBL; AJ459777; CAD31977.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80908.1; -; Genomic_DNA.
DR RefSeq; WP_011278410.1; NC_007181.1.
DR PDB; 1PG5; X-ray; 2.60 A; B=1-164.
DR PDB; 2BE9; X-ray; 2.60 A; B=1-164.
DR PDBsum; 1PG5; -.
DR PDBsum; 2BE9; -.
DR AlphaFoldDB; P74766; -.
DR SMR; P74766; -.
DR IntAct; P74766; 1.
DR STRING; 330779.Saci_1595; -.
DR EnsemblBacteria; AAY80908; AAY80908; Saci_1595.
DR GeneID; 14552088; -.
DR GeneID; 3474278; -.
DR KEGG; sai:Saci_1595; -.
DR PATRIC; fig|330779.12.peg.1535; -.
DR eggNOG; arCOG04229; Archaea.
DR HOGENOM; CLU_128576_0_0_2; -.
DR OMA; CPNRNCI; -.
DR EvolutionaryTrace; P74766; -.
DR Proteomes; UP000001018; 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 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..164
FT /note="Aspartate carbamoyltransferase regulatory chain"
FT /id="PRO_0000142342"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1PG5"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:1PG5"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1PG5"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1PG5"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1PG5"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1PG5"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:1PG5"
SQ SEQUENCE 164 AA; 18280 MW; BA71887C47FCD75B CRC64;
MEIQGNRKEL MVSKIKNGTV IDHIPAGRAF AVLNVLGIKG HEGFRIALVI NVDSKKMGKK
DIVKIEDKEI SDTEANLITL IAPTATINIV REYEVVKKTK LEVPKVVKGI LKCPNPYCIT
SNDVEAIPTF KTLTEKPLKM RCEYCETIID ENEIMSQILG ANNK
