ID   HISZ_PSEMY              Reviewed;         395 AA.
AC   A4XPZ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Pmen_0640;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000680; ABP83408.1; -; Genomic_DNA.
DR   RefSeq; WP_003246505.1; NC_009439.1.
DR   AlphaFoldDB; A4XPZ2; -.
DR   SMR; A4XPZ2; -.
DR   STRING; 399739.Pmen_0640; -.
DR   EnsemblBacteria; ABP83408; ABP83408; Pmen_0640.
DR   KEGG; pmy:Pmen_0640; -.
DR   PATRIC; fig|399739.8.peg.647; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_1_6; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
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_1000016278"
SQ   SEQUENCE   395 AA;  42922 MW;  8B85862A844D6BBB CRC64;
     MATVDRWLLP DGIEEVLPPE AARIEAARRQ VLDLFQRWGY EFVVTPHIEY LESLLTGAGQ
     DLDLRTFKVT DPLSGRQMGF RADITPQVAR IDAHTLRREG PNRLCYAGSV LHAQPRALTT
     SRSPIQLGAE LYGDASPASD IEVISLLVET LELAAVPDVH MDLGHVGIYR GLARAAGLSG
     EVEQQLFDAL QRKAMDEIEA LTAALPAGLG NMLRSLAELC GGREVLDLAQ AALVEAPDAV
     HAALDELVAI ADALELRYPE LPLYFDLGEL RGYNYHTGVV FAAFVPGEGG AIAQGGRYDD
     TGAVFGRARP ATGFSTDLKT LVTLGDMRLD EAVRGVWAPD NHDLYLWQAV RRLRSEGERV
     VQALPGQSEA DAREAGCDRL LALRDGRWQV APLAS