ID   PUR5_ECODH              Reviewed;         345 AA.
AC   B1XAX4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   04-NOV-2026, 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=ECDH10B_2665;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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 + phosphate +
CC         H(+); Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287,
CC         ChEBI:CHEBI:456216; EC=6.3.3.1; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; CP000948; ACB03651.1; -; Genomic_DNA.
DR   RefSeq; WP_001336050.1; NC_010473.1.
DR   AlphaFoldDB; B1XAX4; -.
DR   SMR; B1XAX4; -.
DR   KEGG; ecd:ECDH10B_2665; -.
DR   HOGENOM; CLU_047116_0_0_6; -.
DR   OMA; AACPWSD; -.
DR   UniPathway; UPA00074; UER00129.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:TreeGrafter.
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   GO; GO:0046084; P:adenine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd02196; PurM; 1.
DR   FunFam; 3.30.1330.10:FF:000001; Phosphoribosylformylglycinamidine cyclo-ligase; 1.
DR   FunFam; 3.90.650.10:FF:000001; Phosphoribosylformylglycinamidine cyclo-ligase; 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.
FT   CHAIN           1..345
FT                   /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT                   /id="PRO_1000193015"
SQ   SEQUENCE   345 AA;  36854 MW;  8DA61375E8180401 CRC64;
     MTDKTSLSYK DAGVDIDAGN ALVGRIKGVV KKTRRPEVMG GLGGFGALCA LPQKYREPVL
     VSGTDGVGTK LRLAMDLKRH DTIGIDLVAM CVNDLVVQGA EPLFFLDYYA TGKLDVDTAS
     AVISGIAEGC LQSGCSLVGG ETAEMPGMYH GEDYDVAGFC VGVVEKSEII DGSKVSDGDV
     LIALGSSGPH SNGYSLVRKI LEVSGCDPQT TELDGKPLAD HLLAPTRIYV KSVLELIEKV
     DVHAIAHLTG GGFWENIPRV LPDNTQAVID ESSWQWPEVF NWLQTAGNVE HHEMYRTFNC
     GVGMIIALPA PEVDKALALL NANGENAWKI GIIKASDSEQ RVVIE
//