HISZ_CUPTR
ID HISZ_CUPTR Reviewed; 383 AA.
AC B3R1J2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=RALTA_A1899;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69840.1; -; Genomic_DNA.
DR RefSeq; WP_012353155.1; NC_010528.1.
DR AlphaFoldDB; B3R1J2; -.
DR SMR; B3R1J2; -.
DR STRING; 977880.RALTA_A1899; -.
DR EnsemblBacteria; CAQ69840; CAQ69840; RALTA_A1899.
DR GeneID; 29761185; -.
DR KEGG; cti:RALTA_A1899; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_1_4; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR BioCyc; CTAI977880:RALTA_RS09160-MON; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001692; Chromosome 1.
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 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_1000095456"
SQ SEQUENCE 383 AA; 41586 MW; 4A5F1D065F061D20 CRC64;
MSNHWLLPEN IADVLPSEAR KIEELRRRML DLFRTYGYEL VMPPMLEYLE SLLTGTGHDL
DLRTLKLVDQ LSGRTMGLRA DITPQVARID AHLLNRPGVT RLCYAGNVLH ARPAGFHATR
EPIQIGAEIY GHAGLEADVE IQELMLAALT AAGLSDIRID LCHAGILEAL LAGLPSIRKI
EDALFAALET KDVPALRELT AGMPQTERDA LLALPTLYGG VEVIERARAT LPASPAIGRA
LDELAALAVQ VRGASVNIDL SDLRGYHYHS GVMFAAYVAG LPNYVARGGR YDKVGEAFGR
ARPATGFSLD LREVAALSPV EVRALAIFAP WDADPALRAA IAGLRAGGEI VIQSLPGHTH
ELDEFNCDRQ LVRKDAGWVV VPR