ID   HISZ_SYNPW              Reviewed;         392 AA.
AC   A5GL51;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125};
GN   OrderedLocusNames=SynWH7803_1240;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) 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; CT971583; CAK23666.1; -; Genomic_DNA.
DR   RefSeq; WP_011933146.1; NC_009481.1.
DR   AlphaFoldDB; A5GL51; -.
DR   SMR; A5GL51; -.
DR   STRING; 32051.SynWH7803_1240; -.
DR   EnsemblBacteria; CAK23666; CAK23666; SynWH7803_1240.
DR   KEGG; syx:SynWH7803_1240; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_3; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001566; 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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..392
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000016289"
SQ   SEQUENCE   392 AA;  43509 MW;  5C49C9669C78CC1C CRC64;
     MALQPASGVR DLNPQQVQRN HELREALAAV YRLWGYEEVA PPRIERMDTL KAGGAIDSRD
     IVRLVADEPL GLRPEMTASI ARAACTRFQN RRRPLRLWSH GTVFEGRQAD EGGLCIEEKL
     HCGVELFGAR GVEAELELLS LLMASFKALA LPLSEPPQLL IGHTGLMQLL LKNVDEQDHP
     AYRNCLTQLD RLALRELINT QPQHAHLQQW LDRRGAPDAV ISQLKDAFPD APVLQQLTRL
     INHLSPLAET TGISLQLDPT FQPMYALYDG IVFQLVCRGT SSPVVVARGG RYDTVVQRLG
     ARGKDATGLG FSFCVDDLRD LPGAFAMTTS RTDRILLCYS QNSSMEQALQ AQAGLHRRGL
     SCQVDHHPCE TKAEAEERLR EAGCNSLEWV GD