ID   HISZ_PSEST              Reviewed;         395 AA.
AC   O30548;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; Synonyms=hisX;
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 10701 / JCM 21571 / JM300;
RX   PubMed=9493393; DOI=10.1099/00221287-144-2-569;
RA   Sikorski J., Graupner S., Lorenz M.G., Wackernagel W.;
RT   "Natural genetic transformation of Pseudomonas stutzeri in a non-sterile
RT   soil.";
RL   Microbiology 144:569-576(1998).
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; AF010189; AAC46133.1; -; Genomic_DNA.
DR   RefSeq; WP_014853990.1; NZ_UGVA01000007.1.
DR   AlphaFoldDB; O30548; -.
DR   SMR; O30548; -.
DR   PRIDE; O30548; -.
DR   eggNOG; COG3705; Bacteria.
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_0000171055"
SQ   SEQUENCE   395 AA;  43071 MW;  68FA46C1E7F8FC94 CRC64;
     MATVDRWLLP DGIEEVLPPE AARIETARRR VLDLFQRWGY ELVITPHVEF LESLLSGSGQ
     DLDLKTFKVI DPLSGRQMGL RADITPQVAR VDAHTLRREG PSRLCYAGSV LHAKPRALAT
     SRSPIQLGAE LYGDSSTSSD IEVISLMLEM LELAMVPDVH MDLGHVGIYR GLARAAGLSG
     EAEQRLFDAM QRKAMDEIAE LTATVEPSLA AMLQALARLC GGRETLDAAR RVLAEAPAPV
     TEALEALIRI ADQLALRYPD LPLYFDLGEL RGYHYHTGVV FAVFVPGVGQ SIAQGGRYDD
     IGADFGRARP ATGFSTDLKT LVSLGKAELD SRLSGIWAPY GDDTALWQQI SRLRREGERV
     VQALDGQNGE TAATAGCDRQ LILQDETWTV APLAS