ID   HISZ_PARMW              Reviewed;         392 AA.
AC   Q7U6R1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=SYNW1276;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE07791.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX569692; CAE07791.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011128140.1; NC_005070.1.
DR   AlphaFoldDB; Q7U6R1; -.
DR   SMR; Q7U6R1; -.
DR   STRING; 84588.SYNW1276; -.
DR   EnsemblBacteria; CAE07791; CAE07791; SYNW1276.
DR   KEGG; syw:SYNW1276; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_3; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001422; 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.
FT   CHAIN           1..392
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171070"
SQ   SEQUENCE   392 AA;  43112 MW;  9804FBE28E811586 CRC64;
     MALQPAAGAR DLNPRQVESN RALSERLASV FRLWGYDEVS PPRVERLDTL MAGGAIASED
     VVRLVADEPL GLRPEMTASI ARAACTRLAS RPRPLRLWAS GTVFQSRAAD EGGQCIEENL
     QCGVELFGVA PIEAEMELLS LLMAAVERLD FQAQHQPRLL MGHTGLMDLL LSPVPPVLRD
     AVRAALIQYD RLGLETIELE EGLRATLLSL LDCRGTPNEV LERLSSCFGA QALFDDLHRL
     CRQLQGPAAA QGVRLQLDPT FQPRFELYTG LVFQLVCDTH SAPVVVARGG RYDDLVRRCG
     AQPGQDFGAG FSLAIDPIRE LLSDSSSNPT VAPQLMVAFS ERSTLEAALE RQRWWHQQGR
     SAVIELHPFS TRSLAEQQAT DQGGFQLDWI DP