PUR5_SYNSC
ID PUR5_SYNSC Reviewed; 345 AA.
AC Q3AMJ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, 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=Syncc9605_0414;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) 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 -!- SEQUENCE CAUTION:
CC Sequence=ABB34190.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000110; ABB34190.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041434355.1; NC_007516.1.
DR AlphaFoldDB; Q3AMJ2; -.
DR SMR; Q3AMJ2; -.
DR STRING; 110662.Syncc9605_0414; -.
DR EnsemblBacteria; ABB34190; ABB34190; Syncc9605_0414.
DR KEGG; syd:Syncc9605_0414; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_3; -.
DR OrthoDB; 923547at2; -.
DR UniPathway; UPA00074; UER00129.
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_0000258422"
SQ SEQUENCE 345 AA; 36254 MW; 902811338F574327 CRC64;
MDYKSAGVDV EAGRAFVQRI KASVEATHRP EVIGGLGGFG GLMSLPAGMR KPLLVSGTDG
VGTKLELAQE HGSHHGVGID LVAMCVNDVI TSGAAPLFFL DYMATGALAP SAMAEVVEGI
ADGCRQSGCA LLGGETAEMP GFYPQGRYDI AGFCVAVVEE DELIDGQRIQ PGDSVIGVAS
SGVHSNGFSL VRKVLEKANA DANTVYGDNQ RPLIGDLLAP TTLYADLVQH LMQSGCELHG
MAHITGGGLP ENLPRCLPEG CSARIDASSW TRPTLFRWLQ EAGNIPERDL WHTFNLGIGF
CLVVPARSED AVIEHCRGKN HQAWLIGNVT SNTPGNAAVL EGVPA