HISZ_BACAA
ID HISZ_BACAA Reviewed; 420 AA.
AC C3P500;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=BAA_1491;
OS Bacillus anthracis (strain A0248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=592021;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A0248;
RA Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA Brettin T.;
RT "Genome sequence of Bacillus anthracis A0248.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001598; ACQ49257.1; -; Genomic_DNA.
DR RefSeq; WP_000170328.1; NC_012659.1.
DR AlphaFoldDB; C3P500; -.
DR SMR; C3P500; -.
DR GeneID; 45021403; -.
DR KEGG; bai:BAA_1491; -.
DR HOGENOM; CLU_025113_0_0_9; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
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.
FT CHAIN 1..420
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000122660"
SQ SEQUENCE 420 AA; 48830 MW; 35ECF3E1D86A6289 CRC64;
MTKWKRANPN GTRDYLFEEC TLIEEVEQKL RRTFLERGYE EIRTPTIEFY DVFAFQSRPI
DEEKMYKFFD EKGRIIVLRP DMTIPLARVV GTQRCDTPLK VTYSGNVFRA NESLAGKYNE
IVQSGIEVIG IDNVRAEIEC VISVIQSLQK LRVQSFTIEI GQVQLYKCIV KKLSIHEEEE
KFLRTYIESK NYASLSNFIR DKKLDRCDET VKLLEKLPRL FGNLEVIEEA EKLASSNEMK
MAITRVKEIY EAIEKLGYGS YISIDLGTIQ HLDYYTGVIF KGYIYEIGEE IVSGGRYDEL
IGNFGEMLPA VGLAVQVNQI VKALQEQQEP YERKRIDIMI HYELNRLAEA ERLRNLLQKD
GKKVALSLFS NLNDTFQFAR KNQIVTVVEA KSESLVEYVW KEKWVVQKEG ETSCVTFKLR