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Database: UniProt
Entry: A0A168B550_9HYPO
LinkDB: A0A168B550_9HYPO
Original site: A0A168B550_9HYPO 
ID   A0A168B550_9HYPO        Unreviewed;       314 AA.
AC   A0A168B550;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN   ORFNames=AAL_04917 {ECO:0000313|EMBL:KZZ94806.1};
OS   Moelleriella libera RCEF 2490.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX   NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ94806.1, ECO:0000313|Proteomes:UP000078544};
RN   [1] {ECO:0000313|EMBL:KZZ94806.1, ECO:0000313|Proteomes:UP000078544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ94806.1,
RC   ECO:0000313|Proteomes:UP000078544};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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}.
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:KZZ94806.1}.
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DR   EMBL; AZGY01000010; KZZ94806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168B550; -.
DR   STRING; 1081109.A0A168B550; -.
DR   OrthoDB; 275532at2759; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000078544; 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:KZZ94806.1};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078544};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZZ94806.1}.
FT   DOMAIN          59..235
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
FT   DOMAIN          240..312
FT                   /note="Histidine biosynthesis HisG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08029"
SQ   SEQUENCE   314 AA;  33847 MW;  15D93E1640CF4BCF CRC64;
     MDLANHLEGR LLFAVPKKGR LNQAALNLLE GADIQFRREN RLDIALVKNL PIALVFLPAA
     DIPTFVGQGR VDLGITGWDQ VREHEVVSSP PGSDNAGCEM VMDLGFGSCK LQVQVPENGG
     FAHSRDLIGK SIGTSFVNLA VDYFRKLEAE YDGDKGQETS GRELRTKIIE LSGSVEAACA
     LGVADGIVDL VESGETMRAA GLKAIDTVVE STAVLVKSRS PSNPAMVDLI ASRIRGVIIA
     QRFVLCQYNI ERTRLPDACK ITPGKRAPTI TSLDGEGWVA VSAMVEKKRI ALVMDDLSRV
     GASDILVLDI HNTR
//
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