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HISZ_CUPMC
ID   HISZ_CUPMC              Reviewed;         383 AA.
AC   Q1LLK0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Rmet_2097;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF08976.1; -; Genomic_DNA.
DR   RefSeq; WP_011516810.1; NC_007973.1.
DR   AlphaFoldDB; Q1LLK0; -.
DR   SMR; Q1LLK0; -.
DR   STRING; 266264.Rmet_2097; -.
DR   EnsemblBacteria; ABF08976; ABF08976; Rmet_2097.
DR   KEGG; rme:Rmet_2097; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_1_4; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002429; 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   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..383
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000016282"
SQ   SEQUENCE   383 AA;  41947 MW;  5D389F57C5DC208D CRC64;
     MSNRWLLPEN IADVLPSEAR KIEELRRRML DLFRTYGYEL VMPPMLEYLE SLLTGTGHDL
     DLRTLKLVDQ LSGRTLGLRA DITPQVARID AHLLNRPGVT RLCYAGNVLH ARPAGFNATR
     EPIQIGAEIY GHAGLEADVE IQELMLAALQ VAGLSDIRLD LCHAGILEAL LAALPSIRQI
     EEAMFAALET KDVPALRELT QGLPDTERDA LLALPTLYGG VEVIERARAT LPASPAIGRA
     LDELAALAAQ VSNASVNIDL SDLRGYHYHS GVMFTAYVSG LPNYVARGGR YDKVGEAFGR
     ARPATGFSLD LREVAALSPV EVRAQAIFAP WDADPALRFA ITTLRANGEI VIQSLPGHTH
     ELDEFNCDRQ LQRQGANWVV VPR
 
 
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