ID   HISZ_PSEE4              Reviewed;         395 AA.
AC   Q1I453;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=PSEEN4939;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
CC   -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC       allow the feedback regulation of ATP phosphoribosyltransferase activity
CC       by histidine. {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- MISCELLANEOUS: This function is generally fulfilled by the C-terminal
CC       part of HisG, which is missing in some bacteria such as this one.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       HisZ subfamily. {ECO:0000255|HAMAP-Rule:MF_00125}.
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DR   EMBL; CT573326; CAK17583.1; -; Genomic_DNA.
DR   RefSeq; WP_011535944.1; NC_008027.1.
DR   AlphaFoldDB; Q1I453; -.
DR   SMR; Q1I453; -.
DR   STRING; 384676.PSEEN4939; -.
DR   EnsemblBacteria; CAK17583; CAK17583; PSEEN4939.
DR   KEGG; pen:PSEEN4939; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_1_6; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000658; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00125; HisZ; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   InterPro; IPR004517; HisZ.
DR   PANTHER; PTHR43707; PTHR43707; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT   CHAIN           1..395
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000016277"
SQ   SEQUENCE   395 AA;  43154 MW;  321BC627EDB7E8B2 CRC64;
     MATVDRWLLP DGIEEVLPPE AARIEIARRQ VLDLFQSWGY ELVVTPHIEY LESLLTGAGQ
     DLDQRTFKVV DPQSGRLMGF RADFTPQVAR IDAHTLRREG PSRLCYAGSV LHAQPRALST
     SRSPIQLGAE LYGDASPTSD VEVISLMLAT LQLTDVPDVH MDLGHVGIYR GLARAANLSG
     DVEQQLFDAL QRKAVDEVQT LTADLPKDLG NMLRALVELC GGREVLAEAR VRLGRAPASV
     LAALDDLLAI ADRLASRYPD LPLYFDLGEL RGYHYHTGVV FAVFVPGEGQ SIAQGGRYDD
     IGADFGRARP ATGFSTDLKT LVTLGRAEVV LPAGGIWMPD SSDAALWQHV CQLRNEGQRV
     VQALPGQPLS AALEADCDRQ LIQQDGRWQV LPLTH