PYRI_ERWT9
ID PYRI_ERWT9 Reviewed; 154 AA.
AC B2VL34;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-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=ETA_03620;
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99;
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO95408.1; -; Genomic_DNA.
DR RefSeq; WP_012440123.1; NC_010694.1.
DR AlphaFoldDB; B2VL34; -.
DR SMR; B2VL34; -.
DR STRING; 465817.ETA_03620; -.
DR EnsemblBacteria; CAO95408; CAO95408; ETA_03620.
DR KEGG; eta:ETA_03620; -.
DR eggNOG; COG1781; Bacteria.
DR HOGENOM; CLU_128576_0_0_6; -.
DR OMA; CPNRNCI; -.
DR OrthoDB; 1657328at2; -.
DR Proteomes; UP000001726; 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..154
FT /note="Aspartate carbamoyltransferase regulatory chain"
FT /id="PRO_1000088826"
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 154 AA; 17366 MW; 9D272439E05559C7 CRC64;
MTQDNKLQVE AIKRGTVIDH IPALVGFKLL SLFRLTETDQ RITIGLNLPS GELGRKDLIK
IENTFLTDDQ VNQLAVYAPH ATVNRIDEYN VVAKLSPTLP DRIDRVLTCP NSNCISRSEP
VDSSFAVKKR HDELHLKCKY CEKEFAHHVV MANG
