ID A0A225X605_9STRA Unreviewed; 470 AA.
AC A0A225X605;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE SubName: Full=Phosphoribosyl-ATP diphosphatase {ECO:0000313|EMBL:OWZ24699.1};
GN ORFNames=PHMEG_000222 {ECO:0000313|EMBL:OWZ24699.1};
OS Phytophthora megakarya.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4795 {ECO:0000313|EMBL:OWZ24699.1, ECO:0000313|Proteomes:UP000198211};
RN [1] {ECO:0000313|Proteomes:UP000198211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zdho120 {ECO:0000313|Proteomes:UP000198211};
RA Ali S., Shao J., Larry D.J., Kronmiller B., Shen D., Strem M.D.,
RA Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., Bailey B.A.;
RT "Phytopthora megakarya and P. palmivora, two closely related causual agents
RT of cacao black pod achieved similar genome size and gene model numbers by
RT different mechanisms.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19;
CC Evidence={ECO:0000256|ARBA:ARBA00000024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001460};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000256|ARBA:ARBA00005204}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000256|ARBA:ARBA00005169}.
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:OWZ24699.1}.
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DR EMBL; NBNE01000005; OWZ24699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225X605; -.
DR STRING; 4795.A0A225X605; -.
DR EnsemblProtists; OWZ24699; OWZ24699; PHMEG_000222.
DR OrthoDB; 50870at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000198211; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.287.1080; MazG-like; 1.
DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 1.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR NCBIfam; TIGR03188; histidine_hisI; 1.
DR PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR SUPFAM; SSF141734; HisI-like; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198211}.
FT DOMAIN 265..337
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT REGION 451..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 50379 MW; 5A9515C35F4EE9C5 CRC64;
MLIPVFSSLS SATTDAQCSL LQRLSTLGLV YANLPLHQLR ELAPLVPAFS TEPRELALKA
SLLDARTLLG PFSADMLEPL AAWLDQGIEK VLVDAVSSED AELERVAIAV SELPANRVAL
RIPVPSLHTN EAVQLQQKLA RLTDVACGVV FVIDSPLTQE DGFEALFTSL QVLRKSVDDN
FLFAVEMSAG NADLAVTRIQ ELHHRNIYVV APGYCAGEGE DVAAVVEGEA VVDAALAFVK
CLRTDRPDGL FTTVVADEAG VALGLVYSSA ESIIAAVSSG RGVYYSRSRG GLWKKGESSG
NAQKLIKIDM DCDSDALRFT VNQTGAGFCH LNTRTCWGHD GGFRALESML FSRYEHAPAG
SYTKRLFDDA ELLRNKLVEE AQELAEAESV PDVAGEAADV MYFAMVRCVA AGCKLSDVEK
MLDKRALKVK RRPGNSKAYR ISAANKILNS KGMTSGSASA ASASAVSEQS
//
