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Database: UniProt
Entry: C1GN18_PARBD
LinkDB: C1GN18_PARBD
Original site: C1GN18_PARBD 
ID   C1GN18_PARBD            Unreviewed;       311 AA.
AC   C1GN18;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 2.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN   ORFNames=PADG_08604 {ECO:0000313|EMBL:EEH45020.2};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45020.2, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH45020.2, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH45020.2,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009372}.
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DR   EMBL; KN275984; EEH45020.2; -; Genomic_DNA.
DR   RefSeq; XP_010763967.1; XM_010765665.1.
DR   AlphaFoldDB; C1GN18; -.
DR   STRING; 502780.C1GN18; -.
DR   GeneID; 22586830; -.
DR   KEGG; pbn:PADG_08604; -.
DR   VEuPathDB; FungiDB:PADG_08604; -.
DR   eggNOG; KOG2831; Eukaryota.
DR   HOGENOM; CLU_038115_1_2_1; -.
DR   InParanoid; C1GN18; -.
DR   OMA; ITAKKYV; -.
DR   OrthoDB; 275532at2759; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001628; 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:EEH45020.2};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEH45020.2}.
FT   DOMAIN          68..230
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
FT   DOMAIN          235..307
FT                   /note="Histidine biosynthesis HisG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08029"
SQ   SEQUENCE   311 AA;  33340 MW;  6215359553EBF818 CRC64;
     MDIVNHADDP IDPFQKLRRK QEKREGEGRL QQSAIDLLAG SDIQFRRETR LDIALVKNLP
     IAIIFLPAAD IPTFVGEGRV DLGITGRDQV AEHDANLLPD EVSGVEEMLD LGFGGCKLQV
     QVPQKGLIMD PKELVGKHVV TSFTGLTQGY FAKLEGKQSS STKIKYVGGS VEAACALGVA
     DGIVDLVESG ETMKAAGLKA IGTVVESTAV LVKSRKTTHG LVELIESRIR GVIAAKKYVL
     CQYNVPRPLL AAACEITPGK RAPTVTPIED AGWVAVSSMV EKKSIATVMD QLTIVGATDI
     LVISISNSRT R
//
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