ID   HIS1_MICAN              Reviewed;         216 AA.
AC   B0JK88;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018};
DE            Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018};
DE            EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018};
GN   Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018}; OrderedLocusNames=MAE_61200;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_01018}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01018};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01018}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_01018}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}.
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:0000255|HAMAP-Rule:MF_01018}.
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DR   EMBL; AP009552; BAG05942.1; -; Genomic_DNA.
DR   RefSeq; WP_002797253.1; NC_010296.1.
DR   AlphaFoldDB; B0JK88; -.
DR   SMR; B0JK88; -.
DR   STRING; 449447.MAE_61200; -.
DR   PaxDb; B0JK88; -.
DR   EnsemblBacteria; BAG05942; BAG05942; MAE_61200.
DR   KEGG; mar:MAE_61200; -.
DR   eggNOG; COG0040; Bacteria.
DR   HOGENOM; CLU_038115_2_0_3; -.
DR   OMA; VASKFVH; -.
DR   OrthoDB; 1419568at2; -.
DR   BioCyc; MAER449447:MAE_RS26720-MON; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001510; 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..216
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_1000084158"
SQ   SEQUENCE   216 AA;  23953 MW;  5B68E1D90BAD3632 CRC64;
     MLTIALPKGA LLNESIQIFQ KIGLDFSAFL DSKNRQLQIT DPTNQAKALL VRATDVPVYV
     EYGQAQLGIA GYDVLLEKSP DVANLIDLKF GYCRMSVAVP ADSPYQSPLD IPHHGKVASK
     FVNCAKDYFR RLDIPVEIIP LYGSVELGPI TGMSEAIVDL VSTGRTLREN GLVEIDELFA
     SSARLIAHPL SYRLDRDQIY NWVEKLREPT TSMAKV