PURP_SULTO
ID PURP_SULTO Reviewed; 333 AA.
AC Q975Y9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=STK_02890;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000023; BAB65259.1; -; Genomic_DNA.
DR RefSeq; WP_010978242.1; NC_003106.2.
DR AlphaFoldDB; Q975Y9; -.
DR SMR; Q975Y9; -.
DR STRING; 273063.STK_02890; -.
DR EnsemblBacteria; BAB65259; BAB65259; STK_02890.
DR GeneID; 1458194; -.
DR KEGG; sto:STK_02890; -.
DR PATRIC; fig|273063.9.peg.343; -.
DR eggNOG; arCOG04346; Archaea.
DR OMA; CIHYFYS; -.
DR UniPathway; UPA00074; UER00134.
DR Proteomes; UP000001015; 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; Reference proteome.
FT CHAIN 1..333
FT /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT ribofuranosyl 5'-monophosphate synthetase"
FT /id="PRO_0000348641"
FT DOMAIN 94..324
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 73
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 124..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 230
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 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
SQ SEQUENCE 333 AA; 37892 MW; 204A1E55351DA404 CRC64;
MYILTIGSHS SLQILHGAKK EGFKTALVTP EKRVKFYKQF TFIDEVYGYK NEDEAVDYIN
DFANNGILIP HGSLVEYIGP ERVNKIKTKI FGNRNLFEWE ANQKKKMSLL KSAKIKIPEQ
FENPEDIDRL VIIKLPGAKG GKGYFIARNK SEAKEGLNKL LEQKMIRSID EVIIQEYVIG
VPMYFQFFNS IILNRLEIMG IDIRYETNID GLRRLPADIK IDPTLVVVGN IPAVARESLL
PLVYEYGENF VNTVKELVPP GMIGPFCLES VVTDQGDIVV FEFSGRIVAG TNLYVNGSPY
SWLYWDEPMS VGRRISREIK LAINSNKLEQ VLT
