ID PUR5_SULTO Reviewed; 319 AA. AC Q970V2; F9VNF9; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000255|HAMAP-Rule:MF_00741}; DE EC=6.3.3.1 {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIR synthase {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=AIRS {ECO:0000255|HAMAP-Rule:MF_00741}; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000255|HAMAP-Rule:MF_00741}; GN Name=purM {ECO:0000255|HAMAP-Rule:MF_00741}; GN OrderedLocusNames=STK_14990; OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) OS (Sulfolobus tokodaii). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfurisphaera. OX NCBI_TaxID=273063; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7; RX PubMed=11572479; DOI=10.1093/dnares/8.4.123; RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T., RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.; RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon, RT Sulfolobus tokodaii strain7."; RL DNA Res. 8:123-140(2001). CC -!- CATALYTIC ACTIVITY: CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00741}; 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. {ECO:0000255|HAMAP- CC Rule:MF_00741}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00741}. CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000255|HAMAP- CC Rule:MF_00741}. 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; BA000023; BAK54605.1; -; Genomic_DNA. DR RefSeq; WP_010979549.1; NC_003106.2. DR AlphaFoldDB; Q970V2; -. DR SMR; Q970V2; -. DR STRING; 273063.STK_14990; -. DR GeneID; 42801265; -. DR KEGG; sto:STK_14990; -. DR PATRIC; fig|273063.9.peg.1706; -. DR eggNOG; arCOG00639; Archaea. DR OrthoDB; 6605at2157; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000001015; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule. 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 HAMAP; MF_00741; AIRS; 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 NCBIfam; TIGR00878; purM; 1. 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 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1..319 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_0000148290" SQ SEQUENCE 319 AA; 35044 MW; E2567488BD539165 CRC64; MVSEYKKAGV DLNKLKEYHT LALNTFQNSG VLKIGHYANA IKLDDKYLAM HVDGVGTKTI LALKTGIIEP TGIDCIAMNV NDLVCIGARP LAGVDYLALE KPMDDVVEKV MKGLKQGADE ANIEIIGGET AIMPGVITGY DLSCSVIGIS DRLKTGEDVA PGDVILGLKS NGVHSNGYSL IRKLIDEGKL SLNDWGEELM RPTRIYSSSI IPILDKIKAL AHITGGAFSK LKRITNYRIN LKMPDPPEVF KAIENAGVPH FEMYKIFNMG IGMIIFVSKD LKDDIIEFLS KKETVYELGY VEKGEGIKIT TYKNEILYI //