PYRI_HYPBU
ID PYRI_HYPBU Reviewed; 160 AA.
AC A2BJ23;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002};
GN Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; OrderedLocusNames=Hbut_0109;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
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; CP000493; ABM79984.1; -; Genomic_DNA.
DR RefSeq; WP_011821301.1; NC_008818.1.
DR AlphaFoldDB; A2BJ23; -.
DR SMR; A2BJ23; -.
DR STRING; 415426.Hbut_0109; -.
DR EnsemblBacteria; ABM79984; ABM79984; Hbut_0109.
DR GeneID; 4781406; -.
DR KEGG; hbu:Hbut_0109; -.
DR eggNOG; arCOG04229; Archaea.
DR HOGENOM; CLU_128576_0_0_2; -.
DR OMA; CPNRNCI; -.
DR OrthoDB; 101957at2157; -.
DR Proteomes; UP000002593; 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..160
FT /note="Aspartate carbamoyltransferase regulatory chain"
FT /id="PRO_0000321499"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00002"
SQ SEQUENCE 160 AA; 17564 MW; 8D3B919F51349740 CRC64;
MESGSGLLVR RIREGTVIDH IPAGRALTVL KILGITGREG ARIAVVMNVE SRKLGRKDIV
KIEGRHLSPE EVDKIALVAP RATINIIHDY RVVAKRRVTV PDIVEGILMC PNPSCITRVG
REPVKPRFRV VSRQPLVLQC VYCGTLVSEE DVAEQLAEGG