ID A0A1X1Q5S2_9FIRM Unreviewed; 394 AA.
AC A0A1X1Q5S2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=D081_1213 {ECO:0000313|EMBL:ORU00119.1};
OS Anaerovibrio sp. JC8.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=1240085 {ECO:0000313|EMBL:ORU00119.1, ECO:0000313|Proteomes:UP000192538};
RN [1] {ECO:0000313|EMBL:ORU00119.1, ECO:0000313|Proteomes:UP000192538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC8 {ECO:0000313|EMBL:ORU00119.1,
RC ECO:0000313|Proteomes:UP000192538};
RA Evans P.N., Cheung J.L., Rosewarne C.P., Morrison M.;
RT "Genomic and phenotypic data suggests Anaerovibrio species JC8 from the
RT bovine rumen reduces fumarate and sulphite to decrease the inhibitory
RT effect of hydrogen.";
RL Submitted (OCT-2012) 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:ORU00119.1}.
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DR EMBL; ANBM01000005; ORU00119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1Q5S2; -.
DR STRING; 1240085.D081_1213; -.
DR OrthoDB; 9800814at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000192538; 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:ORU00119.1};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Transferase {ECO:0000313|EMBL:ORU00119.1}.
FT DOMAIN 28..334
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 394 AA; 43889 MW; 0E73F277D47030EA CRC64;
MENRDMVLEI PYGTRDFLPR EAAGKRAIEA AIAEEFNLWG YDEIVTPTVE FLDTLTMGNG
SNLEPHMFKL FDKNNRTMAL RYEMTTPIAR VAASRMKEDK LPLKLSYISS VFRYEQAQTG
RQCEFHQAGV ELLGSDKATA DAEIIALAIS ALKKTGLNDF IICLGQVDFI NGLMKQCGLS
AKEMGNIRAA IENRDLVGLN NIADKADISD DARKMVKEIP LLHGNREILK KAYSMVNNEQ
SRKALDNLSE ICNLLEAYGV SEYITFDLGV IRDFSYYTGM VFEAYTPGLG YPLCGGGRYD
NMLTDFGTDM SATGFAFGIE RVMLALERHG LKAPQTQRDV YVAFAPGKEP EAIKAVQKLR
MAGEACEMAM GPSTEQDAEE YRAGKGYQQL IFVR
//
