ID   HIS1_NOSS1              Reviewed;         214 AA.
AC   Q8YVL0;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=ATP phosphoribosyltransferase;
DE            Short=ATP-PRT;
DE            Short=ATP-PRTase;
DE            EC=2.4.2.17;
GN   Name=hisG; OrderedLocusNames=alr1965;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC       diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial
CC       role in the pathway because the rate of histidine biosynthesis seems to
CC       be controlled primarily by regulation of HisG enzymatic activity (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC         alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:73183; EC=2.4.2.17;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC       HisZ.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BA000019; BAB73664.1; -; Genomic_DNA.
DR   PIR; AG2051; AG2051.
DR   RefSeq; WP_010996129.1; NZ_RSCN01000031.1.
DR   AlphaFoldDB; Q8YVL0; -.
DR   SMR; Q8YVL0; -.
DR   STRING; 103690.17131055; -.
DR   EnsemblBacteria; BAB73664; BAB73664; BAB73664.
DR   KEGG; ana:alr1965; -.
DR   eggNOG; COG0040; Bacteria.
DR   OMA; VASKFVH; -.
DR   OrthoDB; 1419568at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd13595; PBP2_HisGs; 1.
DR   HAMAP; MF_01018; HisG_Short; 1.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
DR   PANTHER; PTHR21403; PTHR21403; 1.
DR   Pfam; PF01634; HisG; 1.
DR   TIGRFAMs; TIGR00070; hisG; 1.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..214
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151892"
SQ   SEQUENCE   214 AA;  23325 MW;  5CC1600F00B2AB7A CRC64;
     MLTVALPKGE LLKNSIRLLQ SVGLDFSAFL DSGNRQLQIT DASGTAKGLL VRGQDVPVYV
     EYGQAQIGII GYDVLREKQP QVAHLVDLQF GYCRMSVAVK ASSPYKSPLD LPAHSRVASK
     YVNSAREFFQ GLDLPVEIVP LYGSVELGPI TGMSEAIVDI VSTGRTLKEN GLVEITTLYE
     STARLIAHPL SYRLNTGNLH QLVEQLREGA LTKV