ID   HISZ_THEPX              Reviewed;         380 AA.
AC   B0K622;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, 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};
GN   OrderedLocusNames=Teth514_0999;
OS   Thermoanaerobacter sp. (strain X514).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter;
OC   unclassified Thermoanaerobacter.
OX   NCBI_TaxID=399726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X514;
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., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT   "Complete sequence of Thermoanaerobacter sp. X514.";
RL   Submitted (JAN-2008) 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; CP000923; ABY92298.1; -; Genomic_DNA.
DR   RefSeq; WP_009052792.1; NC_010320.1.
DR   AlphaFoldDB; B0K622; -.
DR   SMR; B0K622; -.
DR   EnsemblBacteria; ABY92298; ABY92298; Teth514_0999.
DR   KEGG; tex:Teth514_0999; -.
DR   HOGENOM; CLU_025113_0_2_9; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002155; 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; IPR006195; aa-tRNA-synth_II.
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.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT   CHAIN           1..380
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000095474"
SQ   SEQUENCE   380 AA;  44163 MW;  FC7DB8F69698F2FE CRC64;
     MIYLPDGVQD FLPEEYKFKR KIEEKFREVF IKFGYQEIMP PTFEYNDNFS VLFDENNLYR
     FFDKKGNILA LRPDVTTQIA RIVSTKLKGS FPLKLCYVAN VYRYDDPQVG KMREFTQAGI
     ELIGTNHEES DAEIIAVAIE ALKSIGIEDF KVDVGQVEFF KRVVEDLELQ NEEINLLREF
     LQQKNQSAIE EFINDKGIRG KKAKFLSELP LLFGGEEVLK RAKELYDTPK LGETIDYLER
     VYRILKDFGM EEYISFDLGM VQNLNYYTGI IFRCFVKGIG YAICTGGRYD GLLGIFGEHI
     PATGFAISVE RSMLALQKQK KDIIDKSWRV LIKYKENLRS NAYKKATLLR GEGKIVEMYS
     YEKAKHVDEN SFDEIIDMEE