HISZ_RUBXD
ID HISZ_RUBXD Reviewed; 413 AA.
AC Q1AX12;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Rxyl_1100;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) 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; CP000386; ABG04066.1; -; Genomic_DNA.
DR RefSeq; WP_011564084.1; NC_008148.1.
DR AlphaFoldDB; Q1AX12; -.
DR SMR; Q1AX12; -.
DR STRING; 266117.Rxyl_1100; -.
DR EnsemblBacteria; ABG04066; ABG04066; Rxyl_1100.
DR KEGG; rxy:Rxyl_1100; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_0_2_11; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 1236894at2; -.
DR PhylomeDB; Q1AX12; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000006637; 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 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..413
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000203117"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 44328 MW; A645058AE0E3E2AA CRC64;
MRSRAARKFS TTPGTRDVLP PESTRLLDVQ RRVLGRFRLH GFREVITPAL EYAEVVEEAR
LRDSAFKLFD PDNQMLLLRP EMTTPIARLV SQRLRNAPPP FKLSYSLPVY RRSEVGRGQS
AEFHQAGVEV VGSASPGEDA GTIALLVEAL EAAGLGPGED FMVVLGQAAF YRGFLERSCP
EVAPALLSAL AGKDLVRVEE LSRRLPDAVA AGARGIPRLV GPASDGAVLE EAERYASGGG
GAALENLRAI LELLGAHGRL EAVMLDLGLI GRHDYYTGAV YEVYAAGLGF TVANGGRYDN
LLRRFGEPLP ATGFAISLER LVSVLPPERP APLLVLVGED AEAVRAARAL RGEGVPVLHV
SGGLAPEEAE RYARSVDARW VGYPAPGGVK LREVGEGGFW LLAVEEAARR VLG