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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
 
 
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