ID   HISZ_MOOTA              Reviewed;         389 AA.
AC   Q2RGV6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Moth_2037;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC20333.1; -; Genomic_DNA.
DR   RefSeq; WP_011393533.1; NC_007644.1.
DR   RefSeq; YP_430876.1; NC_007644.1.
DR   AlphaFoldDB; Q2RGV6; -.
DR   SMR; Q2RGV6; -.
DR   STRING; 264732.Moth_2037; -.
DR   EnsemblBacteria; ABC20333; ABC20333; Moth_2037.
DR   KEGG; mta:Moth_2037; -.
DR   PATRIC; fig|264732.11.peg.2213; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_9; -.
DR   OMA; ELVMPPM; -.
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; 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..389
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000242841"
SQ   SEQUENCE   389 AA;  41904 MW;  37454A85F918119B CRC64;
     MASNLPLQLP AGVSDLLPPE AAALRQLEQR LLNCFRSWGY QEVMTPTFEF ATTFQAGSPA
     GEEGALYKFI DRQGRVLALR PEMTAPIARL VATSLRRREL PLRLGYSARV FRYEEPQAGR
     RREFHQAGVE LIGAGGVAGD VEIIALAVES LAQAGLEDFR LGLGQVAVTK GVLQDLALPP
     EAVAGIKSAL ASKDLVALER IYDEYHLEGE RRRRLELLAT IHGGREALEE ARACFGRTAA
     AASLAELSRV WEALGAAGLE KWLFIDLGIL RDFDYYTGIV FEGYVPGLGA PVCGGGRYDG
     LLAQFGYPCP ATGFALGLER LLLARGETAP ASLAGGYLVA GRDLAALLKR ARELRSKGTA
     VVLDGESRSR QEAAARAAAR GLNLEWIGE