ID A0A1V4INX8_9CLOT Unreviewed; 418 AA.
AC A0A1V4INX8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:OPJ61544.1};
GN ORFNames=CLORY_22260 {ECO:0000313|EMBL:OPJ61544.1};
OS Clostridium oryzae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1450648 {ECO:0000313|EMBL:OPJ61544.1, ECO:0000313|Proteomes:UP000190080};
RN [1] {ECO:0000313|EMBL:OPJ61544.1, ECO:0000313|Proteomes:UP000190080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28571 {ECO:0000313|EMBL:OPJ61544.1,
RC ECO:0000313|Proteomes:UP000190080};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium oryzae DSM 28571.";
RL Submitted (MAR-2017) 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|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:OPJ61544.1}.
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DR EMBL; MZGV01000021; OPJ61544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4INX8; -.
DR STRING; 1450648.CLORY_22260; -.
DR OrthoDB; 9800814at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000190080; 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:SF6; ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT; 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:OPJ61544.1};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000190080};
KW Transferase {ECO:0000313|EMBL:OPJ61544.1}.
FT DOMAIN 26..418
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 418 AA; 47934 MW; 9A7AC1F746CCE315 CRC64;
MVKWKKNIPE GTRDILFQDC ADKKFIENTL RKIYVDRGFL EVITPTLEFY DVFDGEEQGI
EQEKLYKLFD NHGRILTVRP DITIPIARLS GTKLRDSYYP LRFCYCENVF RANENLNGKR
NEFTQSGVEI IGSADLKADI ELIALAVKAL RETGIENFKI ELGHAEFFKG IVQGLPLDDD
DKEKIRGYIE NKNYGSLGNM LMEKEDILEK KDIEILNLFP SLFGDVSVIN KARKYTNNKK
SEEALNSLEY MYIRLKEMGL SQYIYMDLGM VHHLDYYTGL IFRGYIEGAG DDVLYGGRYD
NLVSNFGVDV PATGFAIDVD GILEVLNKQN RLKHINVNAD YIVHCAVELF NVANNISDKI
VQSGSKCELS LFTDTQDTIE YAEKKKIKNI IFVNSHEEIL LYDTASKVIK KFEAEFII
//
