HIS1_SYNP2
ID HIS1_SYNP2 Reviewed; 210 AA.
AC B1XPZ8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=SYNPCC7002_A0620;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) 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; CP000951; ACA98626.1; -; Genomic_DNA.
DR RefSeq; WP_012306250.1; NC_010475.1.
DR AlphaFoldDB; B1XPZ8; -.
DR SMR; B1XPZ8; -.
DR STRING; 32049.SYNPCC7002_A0620; -.
DR PRIDE; B1XPZ8; -.
DR EnsemblBacteria; ACA98626; ACA98626; SYNPCC7002_A0620.
DR KEGG; syp:SYNPCC7002_A0620; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_3; -.
DR OMA; VASKFVH; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001688; 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..210
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_1000135292"
SQ SEQUENCE 210 AA; 23259 MW; DF20C2A3561ED540 CRC64;
MLTIAIPKGG LLPEAIALLQ QVGLDFSAFL DKKNRQLQIT DPTGTARAML VRTHDVPVYV
EYGQAQLGFA GYDVLREKKP DVANLLDLGF GGCRLSVAVP KASPYKNPRQ LPPNCRVASK
FVNCAKDYFR DLDLPIEVIP LHGSVELGPI TGMSEAIVDL VSTGNTLREN NLEEVEVLFH
STVRLIAHPT SYRANRHNML DWVQKLEQIL