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Database: UniProt
Entry: A0A1D6I6V0_MAIZE
LinkDB: A0A1D6I6V0_MAIZE
Original site: A0A1D6I6V0_MAIZE 
ID   A0A1D6I6V0_MAIZE        Unreviewed;       441 AA.
AC   A0A1D6I6V0;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011946};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN   ORFNames=ZEAMMB73_Zm00001d020908 {ECO:0000313|EMBL:ONM55799.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM55799.1};
RN   [1] {ECO:0000313|EMBL:ONM55799.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM55799.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-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}.
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DR   EMBL; CM007650; ONM55799.1; -; Genomic_DNA.
DR   RefSeq; XP_008650885.1; XM_008652663.1.
DR   AlphaFoldDB; A0A1D6I6V0; -.
DR   SMR; A0A1D6I6V0; -.
DR   IntAct; A0A1D6I6V0; 8.
DR   STRING; 4577.A0A1D6I6V0; -.
DR   PaxDb; 4577-GRMZM2G068862_P01; -.
DR   InParanoid; A0A1D6I6V0; -.
DR   UniPathway; UPA00031; UER00006.
DR   ExpressionAtlas; A0A1D6I6V0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR   CDD; cd13593; PBP2_HisGL3; 1.
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:ONM55799.1};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ONM55799.1}.
FT   DOMAIN          157..333
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
FT   DOMAIN          338..422
FT                   /note="Histidine biosynthesis HisG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08029"
SQ   SEQUENCE   441 AA;  48657 MW;  D6EF0024F325CA76 CRC64;
     MFNVARFTCS VAAEHRRQAP PPHCTERKTA ASRPPTDPTK MPGMLAAQFT ALSLSQSPSP
     QSSLRLAIRP SLAARARFVA PRTAASAAAV SAKPAAVSSP LIEDRTVVRI GLPSKGRMAE
     QTLSLLKSCQ LSVRQLNPRQ YTADIPLIPN LEVWFQRPKD IVRKLQSGDL DLGVVGFDIV
     SEYGNGNEDL VVVHDALEFG HCRLSLAVPK EGIFENIHTM EDLLKMTEWT EERPLRVVTG
     FGYLGNKFLR EKGFKHVRFL SADGALESYP PMGMADAIVD LVSSGTTLRE NNLKEIDGGV
     VLESQATLVA SRKSLHKRKG VLEVTHELLE RLEAHLRATA ELMVTANMRG NSAEEVAERV
     LSQTSIWGLQ GPTVSPVYRR RDGKVDVEYY AINVVVPQKL LYKSIQQLRS IGGSGVLVTK
     LTYIFDEETP RWRNLLSELG L
//
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