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HISZ_SINFN
ID   HISZ_SINFN              Reviewed;         379 AA.
AC   C3MGT3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=NGR_c04020;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24198.1; -; Genomic_DNA.
DR   RefSeq; WP_012706983.1; NC_012587.1.
DR   RefSeq; YP_002824951.1; NC_012587.1.
DR   AlphaFoldDB; C3MGT3; -.
DR   SMR; C3MGT3; -.
DR   STRING; 394.NGR_c04020; -.
DR   EnsemblBacteria; ACP24198; ACP24198; NGR_c04020.
DR   KEGG; rhi:NGR_c04020; -.
DR   PATRIC; fig|394.7.peg.3208; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_6_0_5; -.
DR   OMA; YYTGFEF; -.
DR   OrthoDB; 277998at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001054; 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; 2.
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..379
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000122674"
SQ   SEQUENCE   379 AA;  41472 MW;  AA310D928FCEC572 CRC64;
     MPLINLPAFA GDLLADFERL KTLRVDTPVI QPAEPFLDMA GEDLRRRIFM TQSETGDSLC
     LRPEFTIPVC LRHIETATGT PQRYAYLGEV FRQRREGSSE FYQAGIEDLG DTDTAGADAR
     AIGDAMRVLS NRLANRRLKV TLGDQSVFEA VIAACGLPGG WQKRLIHAFG DPKQLQKLLG
     ELADPKSPGV FGHEVERLAI LGILDDEERL VAHLAETMEA TGYSTNASRS PRDIARRLKE
     KMELATTRLD RAALAVMREF LAFDLPLSEA PAALHAFAKK SRLKIDDALS LFDARVAAIA
     KVGAESDLIR YRAAFGRPLD YYTGLVFEIE AEGAPAVLAG GGRFDRLLTL LGAREHIPAV
     GFSLWLDRIE RAIAAAGGA
 
 
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