ID   A0A1I0KED8_9BACL        Unreviewed;       407 AA.
AC   A0A1I0KED8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=SAMN03159358_4099 {ECO:0000313|EMBL:SEU22537.1};
OS   Paenibacillus sp. NFR01.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1566279 {ECO:0000313|EMBL:SEU22537.1, ECO:0000313|Proteomes:UP000198735};
RN   [1] {ECO:0000313|EMBL:SEU22537.1, ECO:0000313|Proteomes:UP000198735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFR01 {ECO:0000313|EMBL:SEU22537.1,
RC   ECO:0000313|Proteomes:UP000198735};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOIK01000005; SEU22537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0KED8; -.
DR   STRING; 1566279.SAMN03159358_4099; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000198735; 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; IPR006195; aa-tRNA-synth_II.
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.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 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:SEU22537.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198735};
KW   Transferase {ECO:0000313|EMBL:SEU22537.1}.
FT   DOMAIN          39..337
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   407 AA;  45109 MW;  91AE7A452E94F7CD CRC64;
     MKMSKPKGFE KPAGVRDYLP RAVKKLRKIE YDVLHCMSRW GYKQMITPTL EYYDTVGVAS
     STSDQKLYKL LNNRGQALVL RSEMTAPVAR VVSSLLKDEP LPLRLSYHAN VFRAIEEEAG
     REAEFFQTGV ELVGDDSPEA DAEVVALAIA SLQAAGVKSF KIAMGHVGFL NGLFQEAVPG
     LPEAQDELKS HLLGRDYVAF RETLRRLELP EAQKNELSGL LRLRGGKEIC SQALELSSHP
     LARASIEHLC KVWEVLVAYG VSEHVLIDLT MIGDFSYYTG MTFEGYAADL GFPVCSGGRY
     DNLLQQFGRP VPSTGFSLKT NRILDGVAGD GEEEELPVLI QYDALRRTEG LQEAARLRAE
     GRMAVTRLVA ATEDLKDVKR LDTDTLEAEG ERFGEILTFV SFVSEHG
//