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Database: UniProt
Entry: A0A0W8D344_PHYNI
LinkDB: A0A0W8D344_PHYNI
Original site: A0A0W8D344_PHYNI 
ID   A0A0W8D344_PHYNI        Unreviewed;       299 AA.
AC   A0A0W8D344;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN   ORFNames=AM587_10013832 {ECO:0000313|EMBL:KUF90817.1}, AM587_10014484
GN   {ECO:0000313|EMBL:KUF80790.1};
OS   Phytophthora nicotianae (Buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF90817.1, ECO:0000313|Proteomes:UP000052943};
RN   [1] {ECO:0000313|EMBL:KUF90817.1, ECO:0000313|Proteomes:UP000052943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943}, and Race 0
RC   {ECO:0000313|EMBL:KUF90817.1};
RA   Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT   "Genomes and virulence difference between two physiological races of
RT   Phytophthora nicotianae.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000915};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUF90817.1}.
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DR   EMBL; LNFO01004505; KUF80790.1; -; Genomic_DNA.
DR   EMBL; LNFO01001517; KUF90817.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W8D344; -.
DR   STRING; 4790.A0A0W8D344; -.
DR   EnsemblProtists; KUF80790; KUF80790; AM587_10014484.
DR   EnsemblProtists; KUF90817; KUF90817; AM587_10013832.
DR   OMA; ITAKKYV; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000052943; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.70.120; -; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   HAMAP; MF_00079; HisG_Long; 1.
DR   InterPro; IPR020621; ATP-PRT_HisG_long.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR013115; HisG_C.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   NCBIfam; TIGR00070; hisG; 1.
DR   NCBIfam; TIGR03455; HisG_C-term; 1.
DR   PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR   Pfam; PF01634; HisG; 1.
DR   Pfam; PF08029; HisG_C; 1.
DR   SUPFAM; SSF54913; GlnB-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:KUF90817.1};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052943};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUF90817.1}.
FT   DOMAIN          65..219
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
FT   DOMAIN          225..296
FT                   /note="Histidine biosynthesis HisG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08029"
SQ   SEQUENCE   299 AA;  32148 MW;  6959CF91A3492C64 CRC64;
     MSAMPPAPVP KKSDERLLFA VPKKGRLHDK ILKLLKGAGL DYHRPNRVDI ALCSSLPVTL
     VFLPASDIAT YVGEGNLDLG ITGQDIIAES RTKVDELLPL GFGKCSLGVQ TPVKDAIASP
     ELLAGKRIVT SFPEVTREYF KQFETEATGP TKIKYVSGSV EAACSLGLAD GIVDLVETGT
     TMKAAGLELI STILKTQAVL IANPQSARKD LVHKVHQRIL GYITATKYRM VTYNVDKEKL
     DAATKITPGR RSPTVNGLVG GGYAVSAMVE VKDVSDVMDQ LHDVGATDIM IFNIENCRA
//
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