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PURP_METS5
ID   PURP_METS5              Reviewed;         332 AA.
AC   A4YCP2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Msed_0017;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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}.
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DR   EMBL; CP000682; ABP94194.1; -; Genomic_DNA.
DR   RefSeq; WP_011921163.1; NC_009440.1.
DR   AlphaFoldDB; A4YCP2; -.
DR   SMR; A4YCP2; -.
DR   STRING; 399549.Msed_0017; -.
DR   EnsemblBacteria; ABP94194; ABP94194; Msed_0017.
DR   GeneID; 5105156; -.
DR   GeneID; 59456552; -.
DR   KEGG; mse:Msed_0017; -.
DR   eggNOG; arCOG04346; Archaea.
DR   HOGENOM; CLU_065084_0_0_2; -.
DR   OMA; CIHYFYS; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000000242; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..332
FT                   /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT                   ribofuranosyl 5'-monophosphate synthetase"
FT                   /id="PRO_0000348617"
FT   DOMAIN          93..323
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         9
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         72
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         123..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         205
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   332 AA;  37742 MW;  1C7AEF1406695566 CRC64;
     MLLLTLASHS SLQILHGAKR EGFETGIVVN GKREGFYRRF SFIDNFYVYS SEDEAVEKIN
     GTSNSVFVPH GSLIEYIGME RVSRIRTPIF GNRNLFPWES NQSKKMKLLE LSNIKTPMKF
     ENPEDVDRMV IVKLPGAKGG RGYFIGRNKQ EVKEGIRRLQ EKGLINNVEE LIIQEYVIGI
     PMYFQFFYSP MLQRVEMTGI DIRYETNVDG LRRLPSDIKA EPTFVVAGNI PAVARESILP
     SVYEYAENFV KTTKNVVPPG AIGPFCLESI VTDTLDVVVF EFSGRIVAGT NLYVDGSPYS
     WLYWDEPMSV GRRIGREINL AIQKNRLNEV TT
 
 
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