PYRI_PHOLL
ID PYRI_PHOLL Reviewed; 154 AA.
AC Q7MZ14;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain {ECO:0000255|HAMAP-Rule:MF_00002};
GN Name=pyrI {ECO:0000255|HAMAP-Rule:MF_00002}; OrderedLocusNames=plu4497;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571874; CAE16869.1; -; Genomic_DNA.
DR RefSeq; WP_011148577.1; NC_005126.1.
DR AlphaFoldDB; Q7MZ14; -.
DR SMR; Q7MZ14; -.
DR STRING; 243265.plu4497; -.
DR EnsemblBacteria; CAE16869; CAE16869; plu4497.
DR GeneID; 24169604; -.
DR KEGG; plu:plu4497; -.
DR eggNOG; COG1781; Bacteria.
DR HOGENOM; CLU_128576_0_0_6; -.
DR OMA; CPNRNCI; -.
DR OrthoDB; 1657328at2; -.
DR BioCyc; PLUM243265:PLU_RS22200-MON; -.
DR Proteomes; UP000002514; 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_0000142309"
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; 17416 MW; 50905F1BECC6FB28 CRC64;
MTQDHKLQVE AIRCGTVIDH IPAQVGFKLL SLFKLTETDQ RITIGLNLPS NRLGKKDLIK
IENTFLTEQQ ANQLAMYAPN ATVNCIENYE VVKKLPINLP KCIDNVLVCP NSNCISHNEP
VESSFRVKVT VEDVVLTCKY CEKEFDRNVV ILND