PUR5_GEOKA
ID PUR5_GEOKA Reviewed; 346 AA.
AC Q5L3D0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=GK0265;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD74550.1; -; Genomic_DNA.
DR RefSeq; WP_011229774.1; NC_006510.1.
DR PDB; 2Z01; X-ray; 2.20 A; A=1-346.
DR PDBsum; 2Z01; -.
DR AlphaFoldDB; Q5L3D0; -.
DR SMR; Q5L3D0; -.
DR STRING; 235909.GK0265; -.
DR EnsemblBacteria; BAD74550; BAD74550; GK0265.
DR KEGG; gka:GK0265; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_9; -.
DR OMA; EPLFMTD; -.
DR UniPathway; UPA00074; UER00129.
DR EvolutionaryTrace; Q5L3D0; -.
DR Proteomes; UP000001172; 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..346
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000258356"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:2Z01"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 98..110
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 151..162
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2Z01"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:2Z01"
FT STRAND 327..341
FT /evidence="ECO:0007829|PDB:2Z01"
SQ SEQUENCE 346 AA; 36816 MW; 65B292536EB228B9 CRC64;
MAKAYKQAGV DIEAGYQAVA LMKEHVQKTM RPEVLGGIGG FGGLFDLSAL GYRQPVLISG
TDGVGTKLKL AFLLDRHDTI GIDCVAMCVN DIIVQGAEPL FFLDYIACGK AVPEKIAAIV
KGVADGCVEA GCALIGGETA EMPGMYDEDE YDLAGFAVGV AEKERLITGE TIQAGDALVG
LPSSGLHSNG YSLVRRIVFE QAKLSLDEIY EPLDVPLGEE LLKPTRIYAK LLRSVRERFT
IKGMAHITGG GLIENIPRML PPGIGARIQL GSWPILPIFD FLREKGSLEE EEMFSVFNMG
IGLVLAVSPE TAAPLVEWLS ERGEPAYIIG EVAKGAGVSF AGGGRA
