HISZ_BURTA
ID HISZ_BURTA Reviewed; 382 AA.
AC Q2SWD4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=BTH_I2244;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC37640.1; -; Genomic_DNA.
DR RefSeq; WP_009890843.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SWD4; -.
DR SMR; Q2SWD4; -.
DR PRIDE; Q2SWD4; -.
DR EnsemblBacteria; ABC37640; ABC37640; BTH_I2244.
DR KEGG; bte:BTH_I2244; -.
DR HOGENOM; CLU_025113_0_1_4; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001930; Chromosome I.
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.
FT CHAIN 1..382
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242830"
SQ SEQUENCE 382 AA; 41708 MW; E32F5FE934AFD726 CRC64;
MSTWLLPENI ADVLPSEARK IEELRRRLLD RFRSYGYEMV MPPLLEYLES LLTSGGNELR
LRTFKLVDQV SGRTLGLRAD MTPQVARIDA HLLNRQGVTR LCYAGPVLHT RPRGLHASRE
QLQIGAEIYG HAGLEADQEI QQLMLDALHL AGLKKIRLDL CHAGVLAALF ARDAAAAGRG
EALYEALAGK DVPRLNELTD DLGADTRAAL RALPRLYGDA SVLDEARRQL PALPEIARAL
DDLAHLASQV KDAEVAIDLA DLRGYAYHSG AMFAAYVDGV PNAVAHGGRY DHVGQAYGRA
RPATGFSLDL REIARISPVE ARGAAILAPW KQDDALRAAV GALRDAGEVV IQALPGHDHV
LDEFACDRAL VERDGAWVVE PR