ID A0A117N4B9_RHILI Unreviewed; 373 AA.
AC A0A117N4B9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000256|ARBA:ARBA00020397, ECO:0000256|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000256|HAMAP-Rule:MF_00125,
GN ECO:0000313|EMBL:KUM27308.1};
GN ORFNames=AU467_02695 {ECO:0000313|EMBL:KUM27308.1};
OS Rhizobium loti (Mesorhizobium loti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=381 {ECO:0000313|EMBL:KUM27308.1, ECO:0000313|Proteomes:UP000053176};
RN [1] {ECO:0000313|EMBL:KUM27308.1, ECO:0000313|Proteomes:UP000053176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM27308.1,
RC ECO:0000313|Proteomes:UP000053176};
RA Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT efficient symbiont and plant-growth promoting strain isolated from Zn-
RT mining soil using Leucaena leucocephala as a trap plant.";
RL Submitted (DEC-2015) 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:0000256|ARBA:ARBA00025246, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004667, ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000256|ARBA:ARBA00011496, ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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 {ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC HisZ subfamily. {ECO:0000256|ARBA:ARBA00005539, ECO:0000256|HAMAP-
CC Rule:MF_00125}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUM27308.1}.
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DR EMBL; LPWA01000098; KUM27308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117N4B9; -.
DR OrthoDB; 9797914at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000053176; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 2.
DR PIRSF; PIRSF001549; His-tRNA_synth; 2.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00125};
KW Glycosyltransferase {ECO:0000313|EMBL:KUM27308.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_00125}; Transferase {ECO:0000313|EMBL:KUM27308.1}.
FT DOMAIN 7..177
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
FT DOMAIN 241..365
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
SQ SEQUENCE 373 AA; 39851 MW; 9F932F45117523BD CRC64;
MTSRYPAIAA DITKLFAARD THAVEVAVLQ PADPFLDMAG EDLRRRIFLT ESETGKTLCL
RPEFTIPVCL DHIASQAGTP RRYSYLGEVF RQRREGGNEF FQAGIEDLGD RDTAAADARS
LADAHALLSL VLPGQPLAIT LGDQTLFEAV LAALGLPRGW RMRLARAFGS APMLEAALAD
LANPPRNSQL AGPVATLVLD GDAEGLAEHI AMGMEEAGLS ASSGRAPADI ARRLIEKAQL
RSVRLSDEAF SALKGFLEID VAMGGATEAL EKFAADAGLS LGAALENFAA RAKAIEAHGL
PVEKIRYDAA FGRPLDYYTG LVFEIAAENA DRPLVGGGRY DRLLTLLGAK KPIPGVGFSV
WLDRIEALRE GAK
//
