HISZ_BRUAB
ID HISZ_BRUAB Reviewed; 378 AA.
AC Q579Q7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=BruAb2_0183;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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; AE017224; AAX75627.1; -; Genomic_DNA.
DR AlphaFoldDB; Q579Q7; -.
DR SMR; Q579Q7; -.
DR EnsemblBacteria; AAX75627; AAX75627; BruAb2_0183.
DR KEGG; bmb:BruAb2_0183; -.
DR HOGENOM; CLU_025113_6_0_5; -.
DR OMA; YYTGFEF; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000540; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT CHAIN 1..378
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242824"
SQ SEQUENCE 378 AA; 40921 MW; E827A4A65543E4E2 CRC64;
MTMVGSRTSP IFNALRVELN AREAELVEIP LIQPADPFLD MAGEDLRRRI FLTENENGDS
LCLRPEFTIP VCRNHIALNA ATPKRYAYLG EVFRQRRDGA AEFLQAGIED LGAADEAASD
ARSLADALSC VKAIAPDAPL EIVLGDQSVF AGMLKALGLP QGWRKKLLRS FGDAHSMDLA
LAELTGTQRR DPLPESLAVL VAEGDEIGLA RMLEAEMLEA GISPGAGRTP VEIARRLIEK
EDLAATHFPA AALDLLRQFL AIRVSLDMAA VTLRAFAADN ALDLGAVLQK FEARADAIAQ
AGIEMKDIIY DASFGRPLDY YTGLVYEIRD ASNRQDGVLA GGGRYDRLLT MLGACEAIPG
VGFSIWLDRL QALAGEKQ