HISZ_GEOKA
ID HISZ_GEOKA Reviewed; 394 AA.
AC Q5KVC4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=GK3077;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD77362.1; -; Genomic_DNA.
DR RefSeq; WP_011232547.1; NC_006510.1.
DR AlphaFoldDB; Q5KVC4; -.
DR SMR; Q5KVC4; -.
DR STRING; 235909.GK3077; -.
DR PRIDE; Q5KVC4; -.
DR EnsemblBacteria; BAD77362; BAD77362; GK3077.
DR KEGG; gka:GK3077; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_0_9; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001172; 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..394
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242835"
SQ SEQUENCE 394 AA; 44150 MW; FCFEAE63DD78D0D0 CRC64;
MAKKLFMFEK PLGMRDTLPF LYELKKQVRS VMAEEIERWG YEFIETPTLE YYETVGAASA
IADHRLFKLL DQQGHTLVLR PDMTAPIARV AASRLYDDGN PLRLAYNANV FRAQQREGGR
PAEFEQIGVE LIGDGTVTAD AEVISLMVAL LKRTGLGRFS VAVGHIGYVN ALFLEILGNE
ERASVLRRFL YEKNYVGYRE HVKSWPLSSI DQKRLLDLLS LRGGTDVIEQ AKTLVTSEKG
RRAADELAVL MAVLRTYGVA EAVKLDMALV SHMSYYTGIL FEVYAEQVGF PIGNGGRYDD
LLAKFSRPAP ATGFGLRVDR LIEAIGETDV RDDIECIVFS QERLAEAVEL AEAKRAEGKR
VVLQHIAGIR DIDAYSQRYR SIVYLLGRSG RDGQ