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Database: UniProt
Entry: A0A1X7L4C9_9BACL
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ID   A0A1X7L4C9_9BACL        Unreviewed;       406 AA.
AC   A0A1X7L4C9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN06295960_2898 {ECO:0000313|EMBL:SMG48072.1};
OS   Paenibacillus aquistagni.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1852522 {ECO:0000313|EMBL:SMG48072.1, ECO:0000313|Proteomes:UP000193834};
RN   [1] {ECO:0000313|EMBL:SMG48072.1, ECO:0000313|Proteomes:UP000193834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11 {ECO:0000313|EMBL:SMG48072.1,
RC   ECO:0000313|Proteomes:UP000193834};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-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|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; FXAZ01000004; SMG48072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7L4C9; -.
DR   STRING; 1852522.SAMN06295960_2898; -.
DR   OrthoDB; 9800814at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000193834; 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:SMG48072.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193834};
KW   Transferase {ECO:0000313|EMBL:SMG48072.1}.
FT   DOMAIN          39..336
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   406 AA;  46247 MW;  89DAFD846FC63306 CRC64;
     MTKPKMFEKP SGVRDYLPDA VTKLKYIERQ SLNCMSQWGY EQIVTPSMEF YDTVGMASAT
     LDHKLFKLLN QRGTAMVLRS DMTAPIARVA SSLMQEAELP IRLSYHANVF RSMEEDSGRE
     AEFYQTGAEL IGDASPEADA EVIALSISCL QAAGVKQFKV AIGHHGFLHG LLEQYLPDQD
     EVQHQLKQYL VQRDVVGYRE LVQELAIDEV KKGQLNQILR LRGGIPVIAE ARHMAQEESV
     RASLQHLELL WEVLDAYGVA EMCMLDLSMV GDFSYYTGTI FEGYAADQGS PVMSGGRYDN
     LLTQFGRPAP ATGFALKTTR LMDALRLNEA HQASLPVLIQ YDEWRRAEAF QEAARLRAQG
     ERVITRRVNE EEQLEEVERR QDQQLFWRGN RYQEILTFVR FLKEHV
//
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