PUR5_ECOSE
ID PUR5_ECOSE Reviewed; 345 AA.
AC B6I571;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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}; OrderedLocusNames=ECSE_2785;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(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 + 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}.
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DR EMBL; AP009240; BAG78309.1; -; Genomic_DNA.
DR RefSeq; WP_012565160.1; NC_011415.1.
DR AlphaFoldDB; B6I571; -.
DR SMR; B6I571; -.
DR EnsemblBacteria; BAG78309; BAG78309; ECSE_2785.
DR KEGG; ecy:ECSE_2785; -.
DR HOGENOM; CLU_047116_0_0_6; -.
DR OMA; EPLFMTD; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000008199; 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; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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 PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00878; purM; 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_1000193016"
SQ SEQUENCE 345 AA; 36933 MW; 709AFABDFEF23D79 CRC64;
MTDKTSLSYK DAGVDIDAGN ALVGRIKGVV KKTRRPEVMG GLGGFGALYA LPQKYREPVL
VSGTDGVGTK LRLAMDLKRH DTIGIDLVAM CVNDLVVQGA EPLFFLDYYA TGKLDVDTAS
AVISGIAEGC LQSGCSLVGG ETAEMPGMYH GEDYDVAGFC VGVVEKSEII DGSKVSDGDV
LIALGSSGPH SNGYSLVRKI LEVSGCDPQT TELDGKPLAD HLLAPTRIYV KSVLELIEKV
DVHAIAHLTG GGFWENIPRV LPDNTQAVID ESSWQWPEVF NWLQTAGNVE RHEMYRTFNC
GVGMIIALPA PEVDKALALL NANGENAWKI GIIKASDSEQ RVVIE
