PUR5_NEIG1
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 25-MAY-2022, entry version 95.
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=NGO0526;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; 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}.
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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 EnsemblBacteria; AAW89264; AAW89264; 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 OMA; EPLFMTD; -.
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; 3.30.1330.10; -; 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 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
