HISZ_DECAR
ID HISZ_DECAR Reviewed; 384 AA.
AC Q47BS6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Daro_2975;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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; CP000089; AAZ47705.1; -; Genomic_DNA.
DR RefSeq; WP_011288703.1; NC_007298.1.
DR AlphaFoldDB; Q47BS6; -.
DR SMR; Q47BS6; -.
DR STRING; 159087.Daro_2975; -.
DR EnsemblBacteria; AAZ47705; AAZ47705; Daro_2975.
DR KEGG; dar:Daro_2975; -.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT CHAIN 1..384
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000242832"
SQ SEQUENCE 384 AA; 41480 MW; 08368300A4AE96ED CRC64;
MNWLLPEYLA DALPAEAARI ERLRRTVLDH FRSRGFELVM PPMLEYLESL LTGAGQDLKL
RTFKLVDQLS GRTMGVRADI TPQAARIDAH LLNHQGVTRL CYCGNVLHTL PATISAGREP
LQIGAELYGY AGIAADLDVI RLMAGAFDQI KLPIRRIDLG HVGIFRALAE AAGLPQEAED
SVLSLLQTKD VPGLIEACAN VPSPYREALQ RLPQLYGGAD VLERAAAELP PLPAITAALE
GLRHLLVGAP ELPFSIDLSD LRGYHYHNGV VFAAYCDGYP AAIALGGRYD GAGKAFGRAR
PATGFSMDLR EVARLVTVGK SNGAILAPHA GQNKHLAAHI AALREQGEIV VELLHGETAC
EGPLCDRKLA LVGEHWIIEA IQED