HISZ_BURA4
ID HISZ_BURA4 Reviewed; 382 AA.
AC B1YR34;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125};
GN OrderedLocusNames=BamMC406_1713;
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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; CP001025; ACB64198.1; -; Genomic_DNA.
DR RefSeq; WP_012363987.1; NC_010551.1.
DR AlphaFoldDB; B1YR34; -.
DR SMR; B1YR34; -.
DR EnsemblBacteria; ACB64198; ACB64198; BamMC406_1713.
DR KEGG; bac:BamMC406_1713; -.
DR HOGENOM; CLU_025113_0_1_4; -.
DR OMA; ELVMPPM; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001680; 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 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..382
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000095448"
SQ SEQUENCE 382 AA; 41627 MW; 95CB25788AFFC662 CRC64;
MSTWLLPENI ADVLPSEARK IEELRRRLLD RFRSYGYEMV MPPLLEYLES LLTSGGADLR
LRTFKLVDQL SGRTLGLRAD ITPQVARIDA HLLNRQGVTR LCYAGHVMHT RPRGLHATRE
QIQIGAEIYG HAGLEADLEI QQLMLDALHL AGLSRIRLDL CHAGVLAALL ARDPQAAERG
ESLYDALSGK DVPLLNELTD DLGADTRAAL CALPHLYGDA SVLDEARARL PVLPEITRAL
DDLAQLAAQA KGVEVAIDLA DLRGYAYHSG AMFTAYIDGV PNAIARGGRY DHVGQAYGRA
RPATGFSLDL RELARISPIE ARGTAILAPW AQDDALGAAV AALRDAGEVV IQALPGHDHV
LDEFACDRSL VERNGAWVVE PR