HISZ_GLOVI
ID HISZ_GLOVI Reviewed; 392 AA.
AC Q7NHZ4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=glr2390;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC90331.1; -; Genomic_DNA.
DR RefSeq; NP_925336.1; NC_005125.1.
DR RefSeq; WP_011142386.1; NC_005125.1.
DR AlphaFoldDB; Q7NHZ4; -.
DR SMR; Q7NHZ4; -.
DR STRING; 251221.35212958; -.
DR EnsemblBacteria; BAC90331; BAC90331; BAC90331.
DR KEGG; gvi:glr2390; -.
DR PATRIC; fig|251221.4.peg.2429; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_2_3; -.
DR InParanoid; Q7NHZ4; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR PhylomeDB; Q7NHZ4; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000557; 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 HAMAP; MF_00125; HisZ; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
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.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..392
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171036"
SQ SEQUENCE 392 AA; 42421 MW; 67B841AEE9ED71F0 CRC64;
MYQPPTGVRD LLPLDVSQKL WIEQRLQRVF TRWGYQRIIT PTLERMETLQ ASGSVDLQAI
LQLRDAEGVS LGLRPDPTPS LARAVATRLA DAPLPVRLSY QMNVFRSTTQ PQEFYQAGVE
LIGAGGVLAD AEVLLVLAEC LAELAPPDWT LILGAVAFTR SWLAQVAEPA RHRLRRAMAE
LDRVAILAEA GIDEAVRSQL LLLFDLRGEP EMVLSKASSL PMSDAQRAEL AELETLTGWL
RGRSVPVVLD LSLVEAFDYY TGLIFEVSAG GRLIGRGGRY DHLLGSYGKP APGAGFALNL
EALQQVLLPT GKLPGRTVGG GFLVVPDGPD AWEAALAEAD KLRCAPGERV EIELLGRTGE
EAIAHGRALG AAVVRWVHPD GSTTDCDLAV IQ