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PURP_PYRIL
ID   PURP_PYRIL              Reviewed;         333 AA.
AC   A1RQP5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01163};
DE            EC=6.3.4.23 {ECO:0000255|HAMAP-Rule:MF_01163};
DE   AltName: Full=5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate--formate ligase {ECO:0000255|HAMAP-Rule:MF_01163};
GN   Name=purP {ECO:0000255|HAMAP-Rule:MF_01163}; OrderedLocusNames=Pisl_0094;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP- and formate-dependent formylation of 5-
CC       aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate
CC       (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl
CC       5'-monophosphate (FAICAR) in the absence of folates.
CC       {ECO:0000255|HAMAP-Rule:MF_01163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide +
CC         ATP + formate = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC         carboxamide + ADP + phosphate; Xref=Rhea:RHEA:24836,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58467, ChEBI:CHEBI:58475, ChEBI:CHEBI:456216;
CC         EC=6.3.4.23; Evidence={ECO:0000255|HAMAP-Rule:MF_01163};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC       1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate route): step
CC       1/1. {ECO:0000255|HAMAP-Rule:MF_01163}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01163}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABL87277.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000504; ABL87277.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_053240228.1; NC_008701.1.
DR   AlphaFoldDB; A1RQP5; -.
DR   SMR; A1RQP5; -.
DR   STRING; 384616.Pisl_0094; -.
DR   EnsemblBacteria; ABL87277; ABL87277; Pisl_0094.
DR   GeneID; 4616976; -.
DR   KEGG; pis:Pisl_0094; -.
DR   eggNOG; arCOG04346; Archaea.
DR   HOGENOM; CLU_065084_0_0_2; -.
DR   OrthoDB; 21169at2157; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000002595; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01163; IMP_biosynth_PurP; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR023656; IMP_biosynth_PurP.
DR   InterPro; IPR009720; IMP_biosynth_PurP_C.
DR   InterPro; IPR010672; IMP_biosynth_PurP_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR38147; PTHR38147; 1.
DR   Pfam; PF06849; DUF1246; 1.
DR   Pfam; PF06973; DUF1297; 1.
DR   PIRSF; PIRSF004602; ATPgrasp_PurP; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..333
FT                   /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT                   ribofuranosyl 5'-monophosphate synthetase"
FT                   /id="PRO_0000348634"
FT   DOMAIN          106..313
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         20
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         85
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         136..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         229
FT                   /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT                   carboxamide"
FT                   /ligand_id="ChEBI:CHEBI:58475"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         281
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
SQ   SEQUENCE   333 AA;  37993 MW;  D0FE1A2EA510D1BE CRC64;
     MSVLKRYDLE KLAVATVASH TALQILRGAK KYGFRTIAIA GRADVAEFYQ QFNFIDEVWT
     VDFRNFVKAA EKLVEANAVF IPHGSYVEYV GWRQALEAPV PTLGCRELIK WEADQYKKME
     LLQRGGIPTS RVYKTPEEVD RPVIVKLFGA KGGRGYFLAR DREELRRRLA GLSDYIIQEY
     VFGVPAYYHY FSSPVYGRVE VFGADIRYES NVDGRTFGWV EPTFVVVGNL PLVLRESLLP
     TIWKYGVQFA KAVEEVVGCR LAGPYCLESI IRDDMSISVF EFSGRIVAGT NIYMGYGSPY
     SVLYFDRPMD MGERIAHEIR EAARRGRLED LFT
 
 
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