HISZ_THEVB
ID HISZ_THEVB Reviewed; 408 AA.
AC Q8DMD8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=tll0181;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC07734.1; -; Genomic_DNA.
DR RefSeq; NP_680972.1; NC_004113.1.
DR RefSeq; WP_011056036.1; NC_004113.1.
DR AlphaFoldDB; Q8DMD8; -.
DR SMR; Q8DMD8; -.
DR STRING; 197221.22293902; -.
DR EnsemblBacteria; BAC07734; BAC07734; BAC07734.
DR KEGG; tel:tll0181; -.
DR PATRIC; fig|197221.4.peg.187; -.
DR eggNOG; COG3705; Bacteria.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000440; 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; 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..408
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171068"
SQ SEQUENCE 408 AA; 44728 MW; AD5D402CD9A918DC CRC64;
MVYQPACGAR DILPLDVARQ RWLEQRLERV FQSWGYQEII TPTIETLATL TAGGTVHPET
VIQVQGSGDE PLGLRPELTA SIARAAVTRM AGMQLPQRLY YKTNVFRRTT GAELGNQQEF
FQAGVELLGA TGLAADAEIL WLVQECLGVL AVGEAYLLVG DAHLTQQLLG TFPAELQKTV
RQCLANLDRV SLQALPAPWR DRALALFDLR GTPEEVGERL AQWSDVAGVV DRFAQLQQLL
ALVAESLAIT LDLSLVQSFD YYTGIIFEVL IPTETELRLV AQGGRYDQLL SIYHPDGATV
PGIGFVFNVE ALLQAVAIPP AALLAPRSQW LVVPRTANAL AAALHHAQTL RLDGSTRVEL
ALLELTPEQI RAYARDRQIP YIAWIESDAP PQIEALSDGA TSLQIQRV
