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HISZ_MICAN
ID   HISZ_MICAN              Reviewed;         405 AA.
AC   B0JS32;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-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=MAE_41680;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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; AP009552; BAG03990.1; -; Genomic_DNA.
DR   RefSeq; WP_012266851.1; NC_010296.1.
DR   AlphaFoldDB; B0JS32; -.
DR   SMR; B0JS32; -.
DR   STRING; 449447.MAE_41680; -.
DR   PaxDb; B0JS32; -.
DR   EnsemblBacteria; BAG03990; BAG03990; MAE_41680.
DR   KEGG; mar:MAE_41680; -.
DR   PATRIC; fig|449447.4.peg.3771; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_3; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   BioCyc; MAER449447:MAE_RS18035-MON; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001510; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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   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..405
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000076247"
SQ   SEQUENCE   405 AA;  44704 MW;  96C070E85AC59E08 CRC64;
     MIHQPPAGTR DLLPLEVTQK GWINDRLQSV FQRWGYQRIV TSTIEWLDTL TAGGAIDPST
     VIQLHGDSQG LSGLRPELTA SIARSAVTRM SGESYPQRLC YRANVFRRPS AGYHGRQVEF
     YQAGVELLFS GGLLADAEIL LLLADCFDSL AVPNWQIILG EAGLTRSLLS PFPAPLREQV
     KRCLALLDYV SLENLPYPNE TLRQQARQLF HLRGNPEDVL AQVALLAQEE SAQKAVNNLK
     SLVELLNADR SGPFPLILDL SLIQTFDYYT GIVFKAVSDH QQNLSILGQG GRYDQLLGVF
     HPQGQSAPGI GFSLNIEELH ESLLSGQTLP TQAAPLDWLL IPLGNNAQIA TFSKARSLRN
     GDPNLRVAID LGGRSEAQIR TYARDRMIKN LAWVQEDGSV SEESL
 
 
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