HISZ_DESHY
ID HISZ_DESHY Reviewed; 383 AA.
AC Q24QI7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=DSY3916;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE85705.1; -; Genomic_DNA.
DR RefSeq; WP_011461465.1; NC_007907.1.
DR AlphaFoldDB; Q24QI7; -.
DR SMR; Q24QI7; -.
DR STRING; 138119.DSY3916; -.
DR EnsemblBacteria; BAE85705; BAE85705; DSY3916.
DR KEGG; dsy:DSY3916; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_0_9; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001946; 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..383
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000016261"
SQ SEQUENCE 383 AA; 42796 MW; 657B5D6D124E782E CRC64;
MPRSSLGLRI PEGMHDLLPD ELALQEQAET SALDLFKAWA YQKVATPTLE YGACIQPVEE
EGDSFFKLFD RQGHVLVLRP ELTTSIARMV STRMRGTAFP LRLCYAADVF RYSKSHKQEF
RQVGVELIGS ASSAADAEVV ALAIEALRKI GGMDFQINLG HMGIFTGIMA ELGVPQEFQL
HYQEKLARKD FVGIERLVKD YGFETRVQDV LLKLPHLHGK EDMLDQVLEW SRRPSLLEAV
NALRQVYRYL KDFGVQDYVS LDLGILRGFS YYTGAVFEGY VPGVGFPVVE GGRYDALYGD
FGEDAPATGF AINLKAIIEQ MVCSNAERPE VLVYGSDVSK VIAEARKLRQ TGKRVEMCLE
SLTQEQAMES AECKGIKEVV CAR