ID PUR5_NEIG1 Reviewed; 344 AA. AC Q5F973; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 101. 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=NGO0526; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700825 / FA 1090; RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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; AE004969; AAW89264.1; -; Genomic_DNA. DR RefSeq; WP_003691398.1; NC_002946.2. DR RefSeq; YP_207676.1; NC_002946.2. DR PDB; 5VK4; X-ray; 2.65 A; A/B=1-344. DR PDBsum; 5VK4; -. DR AlphaFoldDB; Q5F973; -. DR SMR; Q5F973; -. DR STRING; 242231.NGO_0526; -. DR GeneID; 66752866; -. DR KEGG; ngo:NGO_0526; -. DR PATRIC; fig|242231.10.peg.621; -. DR HOGENOM; CLU_047116_0_0_4; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000535; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1..344 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_0000258373" FT HELIX 16..29 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 54..64 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 68..75 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 81..94 FT /evidence="ECO:0007829|PDB:5VK4" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 99..111 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 114..131 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 134..142 FT /evidence="ECO:0007829|PDB:5VK4" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 152..163 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 178..183 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 192..202 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 216..220 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 228..237 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 250..254 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 255..258 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 289..292 FT /evidence="ECO:0007829|PDB:5VK4" FT TURN 293..295 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:5VK4" FT HELIX 308..320 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 325..333 FT /evidence="ECO:0007829|PDB:5VK4" FT STRAND 340..344 FT /evidence="ECO:0007829|PDB:5VK4" SQ SEQUENCE 344 AA; 36898 MW; 2B0C48782E32F485 CRC64; MSTSLSYRDA GVGIDAGDQL VEKIKPFAKR TMRPEVLGDL GGFGALVEIG KKYQNPVLVS GTDGVGTKLK LAFDWDKHDT VGIDLVAMSV NDILVQGAEP LFFLDYFACG KLDVPRATDV IKGIAQGCEE SGCALIGGET AEMPGMYPVG EYDLAGFAVG VVEKENVITG LSIGAGDVVL GLASNGAHSN GYSLIRKIIE RDNPDLDAEF DNGKTLREAV IAPTRLYVKP ILAALEKFTI KGMAHITGGG ITENVPRVLP KNTVAQIDAE SWELPKLFQW LQKAGNVETQ EMYRTFNCGI GMVVIVAAED ADAVRSFLSG QGETVYRLGC IRERQGNEHQ TQVA //