ID A0A0P0N451_9CREN Unreviewed; 339 AA.
AC A0A0P0N451;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00013047};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
GN ORFNames=Pdsh_06230 {ECO:0000313|EMBL:OWJ54615.1}, Pyrde_1426
GN {ECO:0000313|EMBL:ALL01470.1};
OS Pyrodictium delaneyi.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL01470.1, ECO:0000313|Proteomes:UP000058613};
RN [1] {ECO:0000313|EMBL:ALL01470.1, ECO:0000313|Proteomes:UP000058613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Su06 {ECO:0000313|EMBL:ALL01470.1,
RC ECO:0000313|Proteomes:UP000058613};
RA Jung J.-H., Lin J., Holden J.F., Park C.-S.;
RT "Complete genome sequence of hyperthermophilic archaeon Pyrodictium
RT delaneyi Su06.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OWJ54615.1, ECO:0000313|Proteomes:UP000196694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hulk {ECO:0000313|EMBL:OWJ54615.1,
RC ECO:0000313|Proteomes:UP000196694};
RA Demey L.M., Miller C., Manzella M., Reguera G., Kashefi K.;
RT "The draft genome of the hyperthermophilic archaeon 'Pyrodictium delaneyi
RT strain Hulk', an iron and nitrate reducer, reveals the capacity for sulfate
RT reduction.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004686}.
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DR EMBL; CP013011; ALL01470.1; -; Genomic_DNA.
DR EMBL; NCQP01000003; OWJ54615.1; -; Genomic_DNA.
DR RefSeq; WP_055409483.1; NZ_NCQP01000003.1.
DR AlphaFoldDB; A0A0P0N451; -.
DR STRING; 1273541.Pyrde_1426; -.
DR GeneID; 26099768; -.
DR KEGG; pdl:Pyrde_1426; -.
DR PATRIC; fig|1273541.4.peg.1522; -.
DR OrthoDB; 6605at2157; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000058613; Chromosome.
DR Proteomes; UP000196694; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ALL01470.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 50..152
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 165..324
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 339 AA; 36268 MW; 66EA78E7D12F9134 CRC64;
MARNRSTAET SLSYRDAGVD LDASEALHTL ASRLLAGRRE AYTSSVELAG LELILHVDGV
GTKTLVLEKL GRLRVAGWDC VVMNTNDVAC DAARPLALVD YIAMPRADEA IFREILEGIR
EAAAATGAVL LGGETAILPG LAQGVDVVCT ILAVREPGWR GNRARPGDVL VGLESSGLHA
NGYSLARRII EERLGGYTAE IEGLDLAEEL SKPVKDYTGF LLEAWSQGLV IAAAHITGGA
FTKMKRILPS GATAVMKMPK PPRIFQVLME AGNVEPSEAY RVWNMGIGLV VAAPRESVDE
LLDLAEKHGH KPHVLGLIEQ GRDGARILLD TPYGKVAYS
//