ID A0A0M8K9D9_9CHLR Unreviewed; 411 AA.
AC A0A0M8K9D9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:GAP64435.1};
GN ORFNames=ARMA_2858 {ECO:0000313|EMBL:GAP64435.1};
OS Ardenticatena maritima.
OC Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC Ardenticatenaceae; Ardenticatena.
OX NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP64435.1, ECO:0000313|Proteomes:UP000037784};
RN [1] {ECO:0000313|EMBL:GAP64435.1, ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:GAP64435.1,
RC ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL Genome Announc. 3:e01145-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT Ardenticatena maritima Strain 110S.";
RL Submitted (AUG-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:GAP64435.1}.
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DR EMBL; BBZA01000265; GAP64435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8K9D9; -.
DR STRING; 872965.SE16_06120; -.
DR InParanoid; A0A0M8K9D9; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000037784; 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|HAMAP-Rule:MF_00125};
KW Glycosyltransferase {ECO:0000313|EMBL:GAP64435.1};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000037784};
KW Transferase {ECO:0000313|EMBL:GAP64435.1}.
FT DOMAIN 35..346
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 411 AA; 45199 MW; EEB144DD39CEB3A1 CRC64;
MMNHSTPSRT THLLRLLPPG VRDIFGDEAA RLTLVHRAAE ETFWRWGYAP VVLPTFEYYD
VLARGFDEQA SGKMHRFIDA QGNLLALRPD LTVPVARLVA SRLVQEPPPV RLAYVAPVFR
YVEPRAGQQR EFREIWQAGV ECVGVNNADA DAEIIALHVA TLQAMGVPRF QLNLGHMGFV
HGVFDALDKQ PPNLAAIRRA IDRKNRHILA EELDRAGVRG AARAALEALP TLWGQGDVLE
RAAALAPTPR ARSAIERLQQ IVARLEAYGV RDFVTIDLGE VRGMHYYTGI TFETFAPHSG
YPIAGGGRYD NLLALYGYDA PAVGFAVFTQ RVLDVLEAEN AAPDVPRPDA LMVACGHAEC
LADLQRRRAA GQRIELDLSS RSPEGTRRKA AARGIGAVLV CGEWQEVAHG D
//