ID HISZ_CLOBL Reviewed; 422 AA.
AC A7GDQ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=CLI_1647;
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F;
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000728; ABS41273.1; -; Genomic_DNA.
DR RefSeq; WP_012099669.1; NC_009699.1.
DR AlphaFoldDB; A7GDQ0; -.
DR SMR; A7GDQ0; -.
DR KEGG; cbf:CLI_1647; -.
DR HOGENOM; CLU_025113_0_0_9; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000002410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 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 NCBIfam; TIGR00443; hisZ_biosyn_reg; 1.
DR PANTHER; PTHR11476:SF7; HISTIDINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT CHAIN 1..422
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000016258"
SQ SEQUENCE 422 AA; 48651 MW; 2E14429AA1E602B8 CRC64;
MENWNKYIPE GMKDILFEES NIKLNIEDQL RKIYKYSGFS EIISPTIEFY DVFNSNIQAI
PQEKMYKLFD NLGRILVLRP DMTTPIGRIT GTKMKDCTYP LKLCYTANIF RVNEKLNGKR
GEITQSGIEI IGTNGIKSDV DSIVTAINTL LSLGLKNFKI ELGEAGFFQA LTENMEIKEE
NLKKLKEIIR NKNYVALKKF LDEISSKYSK EDFELIKNLP KLFGDIKIIE KAKALTKNKK
ALKSLDDIYN IYKSIENIGL EAYISIDLGM VQNIDYYTGV IFKGYVEEVG DSILSGGRYD
NLIQHFGIEL PATGFAINVD DIMIALKKQN TMSMDKDKKV LIFYKEEFLR KAYDFMQELK
MKKIICELSL LDDDKEILLY SKKKGIDFII GFMGEEKLFV KDLKSDKIAF LKKDEIENLL
ML
//
