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HISZ_SYNY3
ID   HISZ_SYNY3              Reviewed;         401 AA.
AC   P74592;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; Synonyms=hisS2; OrderedLocusNames=slr1560;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18700.1; -; Genomic_DNA.
DR   PIR; S76788; S76788.
DR   AlphaFoldDB; P74592; -.
DR   SMR; P74592; -.
DR   STRING; 1148.1653789; -.
DR   PaxDb; P74592; -.
DR   EnsemblBacteria; BAA18700; BAA18700; BAA18700.
DR   KEGG; syn:slr1560; -.
DR   eggNOG; COG3705; Bacteria.
DR   InParanoid; P74592; -.
DR   OMA; ELVMPPM; -.
DR   PhylomeDB; P74592; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001425; Chromosome.
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   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00125; HisZ; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
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.
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..401
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171071"
SQ   SEQUENCE   401 AA;  44282 MW;  488ABA54BAE477FD CRC64;
     MIHHPPAGAR DLLPLEVAQK ARINDQLQQT FHRWGYQRIV TSTLEWLDTL VAGGAISANN
     VIQLQDSGEG RLGLRPELTA SIARAVVTRM TDNQPQRLCY RANVFRNPPE GYHGKQMEFF
     QAGIELLFAG GVRADAEILL LLTDCLTQLG LSDWQLILGD AGLTRSLLAK LPPTLQATVR
     DCITRLDYVE LSQLPYPDNE AKNLALQLFD LRGTVEEVLA RLGKLDLQGE CLGLVDRLQA
     LLCLVAASGD GPANLVLDLS WLQPFDYYTG MVFQAVSRQA DNCYVLGQGG RYDQLLSQYH
     PQQQSFPGTG FSLNIEELHQ CLLELGTLPT STAPIDYLVC PVDDTAEGAT FRHAQQLRRQ
     HPDRRVELDL GGRSPEELNT YAQAMAVGQI VWVGADGPVD L
 
 
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