ID PUR5_ALKEH Reviewed; 347 AA. AC Q0ABB7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 90. 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=Mlg_0516; OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; OC Ectothiorhodospiraceae; Alkalilimnicola. OX NCBI_TaxID=187272; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.; RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1."; RL Submitted (AUG-2006) 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; CP000453; ABI55870.1; -; Genomic_DNA. DR RefSeq; WP_011628265.1; NC_008340.1. DR AlphaFoldDB; Q0ABB7; -. DR SMR; Q0ABB7; -. DR KEGG; aeh:Mlg_0516; -. DR eggNOG; COG0150; Bacteria. DR HOGENOM; CLU_047116_0_0_6; -. DR OrthoDB; 9777881at2; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000001962; 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..347 FT /note="Phosphoribosylformylglycinamidine cyclo-ligase" FT /id="PRO_1000062155" SQ SEQUENCE 347 AA; 36586 MW; DE6866C06524B99A CRC64; MGPDQEGLTY KAAGVDIDAG NELVDRIRDD VKRTMRPGVL GGLGGFGGLF EVPVDRYRRP VLVSGTDGVG TKLKLAIETG RHDGIGIDLV AMCANDVLVT GAEPLYFLDY YATGRLDVEV AAAVIRGIAE GCHQAGAALI GGETAEMPGM YAEGHYDLAG FCVGVVEKDE IIDGSRVGAG DALIALAASG PHSNGYSLIR KVLERAPEGA ATEVDGQPVA DLLMAPTRIY AKPVLDLIRN LPVHAMAHIT GGGLPENLPR VLPEGLGAKL QPWSWPPVFR WLQQTGQIAE AEMLRTFNCG VGMVLVVPAE QADAALQRLR QTGETAWRLG EIGTHEAGAP RVQVVAA //