HISZ_DEIRA
ID HISZ_DEIRA Reviewed; 406 AA.
AC Q9RUE3;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN Name=hisZ; OrderedLocusNames=DR_1444;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC allow the feedback regulation of ATP phosphoribosyltransferase activity
CC by histidine (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000305}.
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DR EMBL; AE000513; AAF11015.1; -; Genomic_DNA.
DR PIR; B75394; B75394.
DR RefSeq; NP_295167.1; NC_001263.1.
DR RefSeq; WP_010888083.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RUE3; -.
DR SMR; Q9RUE3; -.
DR STRING; 243230.DR_1444; -.
DR EnsemblBacteria; AAF11015; AAF11015; DR_1444.
DR KEGG; dra:DR_1444; -.
DR PATRIC; fig|243230.17.peg.1641; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_2_0; -.
DR InParanoid; Q9RUE3; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00773; HisRS-like_core; 1.
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 SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..406
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171034"
SQ SEQUENCE 406 AA; 42851 MW; 9ED6B64D9676E67E CRC64;
MRRVSVSDPL PFSAPLAAGG EALSTSALPA GVRDVLPAEW ERREHLRSHL SALLRSWGYR
GVDLPALELA DPAHPQGNHA FKLIDSGGQV LALRSEYTTA LGRLVGTHFP SGPFPLRLQY
GGRLWLRTQT SELGRLREFN QVGAELIGVT GVQADAELLA LAHAALGQAG VQAQLEVGFP
GFVDAALTDA GLPGPVRAAL HDAIDRKSGA DLDLLARQHG VSPEVTRTLH SLTELYGGPE
VLTEARVLAR GVRAEQAVEH LSAVHAAAQE AGVELLFDLG VSRRYGYYTG LTFRAYVDGI
NQPVLGGGRY ALPGGLPGAG FAIGLERLAA VMPAGVPSEP ETVLALDFAA ATAARAAGLG
AELAWTGDEA ELRHYAQARG LRRWVQGAEL RDVTPADLKI ATEVNA