HISZ_CHESB
ID HISZ_CHESB Reviewed; 373 AA.
AC Q11LA1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Meso_0420;
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans; unclassified Chelativorans.
OX NCBI_TaxID=266779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BNC1;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
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; CP000390; ABG61824.1; -; Genomic_DNA.
DR RefSeq; WP_011579767.1; NC_008254.1.
DR AlphaFoldDB; Q11LA1; -.
DR SMR; Q11LA1; -.
DR STRING; 266779.Meso_0420; -.
DR EnsemblBacteria; ABG61824; ABG61824; Meso_0420.
DR KEGG; mes:Meso_0420; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_6_0_5; -.
DR OMA; YYTGFEF; -.
DR OrthoDB; 277998at2; -.
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 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; 2.
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..373
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_1000016269"
SQ SEQUENCE 373 AA; 40855 MW; 536B20443B15C07A CRC64;
MTSRYPSFAA EILDLFAERE AVLTDIAIIQ PADPFLDMAG EDLRRRIFLT ESETGETLCL
RPEFTIPVCL DHIEKRASTP RRYAYLGEVF RQHREGSPEF FQAGVEDLGA KDRPAADARS
LADARAILSC VLPNTGFHVT LGDQAVFEAV LSALGLPRGW QKRLARAFGS PAMLEAAIAE
FTSPQGTANL PREVASLVAQ GNEQRLTHHI EEAMQAAGHS PTAGREPDEI ARRLLEKAAL
RSVRLSDAAL NALKSFLAIK VPLEQAGERL TAFADEAGIF LDEALADFSA RAERIGDHAL
PLDEIRYDAG FGRPLDYYTG FIFEIGVEGL RQPLVGGGRY DRLLTLLGAE EPIPGVGFSM
WLDRIATVRG EKP