ID A0A1I2YA91_9GAMM Unreviewed; 398 AA.
AC A0A1I2YA91;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ORFNames=DFO67_101261 {ECO:0000313|EMBL:TDX32965.1},
GN SAMN04487959_101259 {ECO:0000313|EMBL:SFH21281.1};
OS Halomonas xianhensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=442341 {ECO:0000313|EMBL:SFH21281.1, ECO:0000313|Proteomes:UP000199040};
RN [1] {ECO:0000313|EMBL:SFH21281.1, ECO:0000313|Proteomes:UP000199040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6848 {ECO:0000313|EMBL:SFH21281.1,
RC ECO:0000313|Proteomes:UP000199040};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TDX32965.1, ECO:0000313|Proteomes:UP000294489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6_TX {ECO:0000313|EMBL:TDX32965.1,
RC ECO:0000313|Proteomes:UP000294489};
RA Lamendella R.;
RT "Freshwater and sediment microbial communities from various areas in North
RT America, analyzing microbe dynamics in response to fracking.";
RL Submitted (MAR-2019) 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}.
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DR EMBL; FOPY01000001; SFH21281.1; -; Genomic_DNA.
DR EMBL; SOEC01000001; TDX32965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2YA91; -.
DR STRING; 442341.SAMN04487959_101259; -.
DR OrthoDB; 9769617at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000199040; Unassembled WGS sequence.
DR Proteomes; UP000294489; 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 CDD; cd00773; HisRS-like_core; 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 NCBIfam; TIGR00443; hisZ_biosyn_reg; 1.
DR PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
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:SFH21281.1};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000199040};
KW Transferase {ECO:0000313|EMBL:SFH21281.1}.
FT DOMAIN 12..322
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
SQ SEQUENCE 398 AA; 43406 MW; 97D5CC439A649ABC CRC64;
MTIADRWLLP DGMDEVLPPQ ATRMETLRRA LLDLYYRWGY DLVMPPPVEF LDSLLTGTGT
DLDLQTFKLT DQLTGRLMGA SADVTPQVAR MDAHSLKRQG PARLCYCSHV LRAKADQHQG
GRSPVQVGVE LFGHAGLEAD LEILRLALSS LTTAGASEIH LALGHIGIYR ALVQLANLQE
DARRALFEAI ERKSPSEVRT LVAMHVADAG LAEMFSALVN LHGGEETIEA ARGALVDAPA
EVVEALDQLQ SLCQGVKRDY PDVTLYIDLA DLRGYQYHTG MMFAAYVPGY GQALAKGGRY
DDTGRAFGRA RPATGFSMDL KLLATLVEQA PQADGIWAPT MATSETEAQQ LNAAIAHLRN
AGERVVQALP DQQTGPAEHR CNRQLVRLGD DWQVSPLT
//
