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