HIS1_SYNSC
ID HIS1_SYNSC Reviewed; 216 AA.
AC Q3AL07;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
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};
GN OrderedLocusNames=Syncc9605_0967;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000110; ABB34725.1; -; Genomic_DNA.
DR RefSeq; WP_011363949.1; NC_007516.1.
DR AlphaFoldDB; Q3AL07; -.
DR SMR; Q3AL07; -.
DR STRING; 110662.Syncc9605_0967; -.
DR EnsemblBacteria; ABB34725; ABB34725; Syncc9605_0967.
DR KEGG; syd:Syncc9605_0967; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_3; -.
DR OMA; VASKFVH; -.
DR OrthoDB; 1419568at2; -.
DR UniPathway; UPA00031; UER00006.
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; Transferase.
FT CHAIN 1..216
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_1000063317"
SQ SEQUENCE 216 AA; 22825 MW; 2A78DD0A50B144AA CRC64;
MITVALAKGA LLKDSVARFA AAGLDFSAVL DKDNRQLMVP TPCGRARALL VRNGDVPTYV
SYGQAQLGVV GFDVLKEHQL PVAQLVDLGF GGCRMAVAVQ ESSGYTRAAD LPAHCRVASK
FTQCAREYFD ALDLPVELVH LNGSVELGPI TGMSEAIVDL VATGRTLREN GLIAIEDLFH
STARLVGHPL SVRLDNGPLA SIVDAIRAAT PVGSFS