HISZ_CUPPJ
ID HISZ_CUPPJ Reviewed; 383 AA.
AC Q46ZJ2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-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=Reut_A2077;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ61441.1; -; Genomic_DNA.
DR RefSeq; WP_011298239.1; NC_007347.1.
DR AlphaFoldDB; Q46ZJ2; -.
DR SMR; Q46ZJ2; -.
DR STRING; 264198.Reut_A2077; -.
DR EnsemblBacteria; AAZ61441; AAZ61441; Reut_A2077.
DR KEGG; reu:Reut_A2077; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_4; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT CHAIN 1..383
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242853"
SQ SEQUENCE 383 AA; 41810 MW; 51DF2627AD11759B CRC64;
MSNHWLLPEN IADVLPSEAR KIEELRRRML DLFRTYGYEL VMPPMLEYLE SLLTGTGHDL
DLRTLKLVDQ LSGRTMGLRA DITPQVARID AHLLNRPGVT RLCYAGNVLH ARPAGFHATR
EPIQVGAEIY GHAGLEADVE IQELMLAALQ AAGLSDIRID LCHAGILEAL LDGLPSIRRI
EDALFAALET KDVSALREIT QGMPQTERDA LLALPTLYGG VEVIDRARAT LPASPAIGRA
LDELVALATQ VRGASINIDL SDLRGYHYHS GVMFAAYVAG LPNYVARGGR YDKVGEAFGR
ARPATGFSLD LREVAALSPI EVRAQAIFAP WDADPALRAA IVALRAAGEI VIQSLPGHTK
ELDEFNCDRQ LVRQEAGWVV APR