HISZ_DESRM
ID HISZ_DESRM Reviewed; 401 AA.
AC A4J716;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Dred_2359;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-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; CP000612; ABO50869.1; -; Genomic_DNA.
DR RefSeq; WP_011878667.1; NC_009253.1.
DR AlphaFoldDB; A4J716; -.
DR SMR; A4J716; -.
DR STRING; 349161.Dred_2359; -.
DR EnsemblBacteria; ABO50869; ABO50869; Dred_2359.
DR KEGG; drm:Dred_2359; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_0_2_9; -.
DR OMA; HQCDFDI; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001556; 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..401
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000117676"
SQ SEQUENCE 401 AA; 44665 MW; 154D23A6568FE658 CRC64;
MTSSRFGRLA PGVRDVLPAE AHLMRGLKEK FTKLVETWGY KEVVTPTFEY MENLASEELQ
EEKFFKFLDR QGHLMALRPD MTRPMARLVA TRMKGITPPL RLFYLANVFN YEQPQVGRQR
EFYQAGVELM GPSSPEADAE VVAMVAEYLM QTGLADFQIS IGNVGIFHGL VKQLGLPKEV
AQELKEALGN KDFVKVEEIL GSHAATPEEA RRTLDLIELR GGPEILDRAF GLAQPGPAAD
AIDNLRQLYW GLTCYGVERH ITLDLGLLRG LDYYTGLVFE GYTVAMGFPI CGGGRYNQLL
AKFGLPMPAT GFAVNLERVL VALERLQGPP REPVPDVLVA WEDNSLANAL QCVKELRYQG
LKVVTAMFEY PPAKAKAEAR SLGASRVIYF DKEGKSEELS L
