ID   HISZ_RHILW              Reviewed;         373 AA.
AC   B5ZRD1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Rleg2_0465;
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304;
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(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; CP001191; ACI53763.1; -; Genomic_DNA.
DR   RefSeq; WP_012556710.1; NC_011369.1.
DR   AlphaFoldDB; B5ZRD1; -.
DR   SMR; B5ZRD1; -.
DR   STRING; 395492.Rleg2_0465; -.
DR   EnsemblBacteria; ACI53763; ACI53763; Rleg2_0465.
DR   KEGG; rlt:Rleg2_0465; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_6_0_5; -.
DR   OMA; YYTGFEF; -.
DR   OrthoDB; 277998at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000008330; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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; 2.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT   CHAIN           1..373
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000095470"
SQ   SEQUENCE   373 AA;  40308 MW;  803251672866C8E9 CRC64;
     MPLINLPEFA SDLLAEFDAR KVERIDTPVI QPAEPFLDIA GEDLRRRIFM TESETGASLC
     LRPEFTIPVC LRHIETATGT PKRYAYLGEV FRQRRDGANE FYQAGIEDLG DINIPSADAR
     AIGDATGILA RLLPGRRLSV TLGDQAVFEA VVQALGLPLG WQKRLIHAFG NMTQLEALLA
     GLVSPQFVTG LDDDVAKLVA SGDEQALVSH LEQEMQATGY SANAGRSPLE IARRLKEKLI
     LSETRLDDAA FHVLEEFLSL DVPLVNASAA LAGFADAAGL KLGNALSRFN GRVAALADAG
     VDLSCLDYRA AFGRPLDYYT GLVFEVTVEG SAAVLAGGGR FDKLLTFLGA TDRIPAVGFS
     FWLDRIETER AAV