ID A0A059LSH7_9CHLO Unreviewed; 364 AA.
AC A0A059LSH7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase domain-containing protein {ECO:0000259|Pfam:PF01502};
DE Flags: Fragment;
GN ORFNames=H632_c30p0 {ECO:0000313|EMBL:KDD77055.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD77055.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD77055.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD77055.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
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:KDD77055.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYPS01000030; KDD77055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LSH7; -.
DR STRING; 1291522.A0A059LSH7; -.
DR OrthoDB; 1114at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000026042; 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 CDD; cd11534; NTP-PPase_HisIE_like; 1.
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:UP000026042}.
FT DOMAIN 1..74
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT NON_TER 364
FT /evidence="ECO:0000313|EMBL:KDD77055.1"
SQ SEQUENCE 364 AA; 39216 MW; F69129804D98ABE3 CRC64;
MQAFADRAAI VETMETGLAT FYSRSRKGRW CKGETSGHFI RVHSVLVDCD ADSVIYVSSA
HGPACHTGAQ SCYYRLLGGG EGAGEQDVNA SLPALVALNR TVLARASEPA GGGKPSWTAK
LLRDPELNCR KVREEADELC RTWEDAEGPE RAASEAADLI YHALVLLRTQ VVVVSLESRG
LSVDWEDDSK ALQCSLFFPA KVFHDLKVQV RQQMATSYGR LLDAALLLSA SSGAAIKLEY
PGPEGSLVVS QAQVHVGLAV PLLHSSLAPL SAPQPSPLSD LWTEPSCAFV CPGHLLREAL
EDLEALAAPI RLELRGEAEG VSLEARAPEA RAGVELPRSV LRAWEGAERA PAHEYRARHL
QLAL
//
