PURP_PYRFU
ID PURP_PYRFU Reviewed; 334 AA.
AC Q8U0R7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=PF1517;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH ATP AND SUBSTRATE
RP AICAR, AND SUBUNIT.
RX PubMed=18069798; DOI=10.1021/bi701406g;
RA Zhang Y., White R.H., Ealick S.E.;
RT "Crystal structure and function of 5-formaminoimidazole-4-carboxamide
RT ribonucleotide synthetase from Methanocaldococcus jannaschii.";
RL Biochemistry 47:205-217(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 -!- SUBUNIT: Homotrimer and homohexamer. {ECO:0000269|PubMed:18069798}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000255|HAMAP-Rule:MF_01163}.
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DR EMBL; AE009950; AAL81641.1; -; Genomic_DNA.
DR RefSeq; WP_011012664.1; NZ_CP023154.1.
DR PDB; 2R84; X-ray; 1.90 A; A/B=1-334.
DR PDB; 2R85; X-ray; 1.70 A; A/B=1-334.
DR PDB; 2R86; X-ray; 2.50 A; A/B=1-334.
DR PDB; 2R87; X-ray; 2.30 A; A/B/C/D/E/F=1-334.
DR PDBsum; 2R84; -.
DR PDBsum; 2R85; -.
DR PDBsum; 2R86; -.
DR PDBsum; 2R87; -.
DR AlphaFoldDB; Q8U0R7; -.
DR SMR; Q8U0R7; -.
DR STRING; 186497.PF1517; -.
DR EnsemblBacteria; AAL81641; AAL81641; PF1517.
DR GeneID; 41713336; -.
DR KEGG; pfu:PF1517; -.
DR PATRIC; fig|186497.12.peg.1580; -.
DR eggNOG; arCOG04346; Archaea.
DR HOGENOM; CLU_065084_0_0_2; -.
DR OMA; VKPHGAK; -.
DR OrthoDB; 21169at2157; -.
DR PhylomeDB; Q8U0R7; -.
DR UniPathway; UPA00074; UER00134.
DR EvolutionaryTrace; Q8U0R7; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..334
FT /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT ribofuranosyl 5'-monophosphate synthetase"
FT /id="PRO_0000348636"
FT DOMAIN 78..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 10
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 11
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 71
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 75
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 132..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 173..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 232
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2R87"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2R85"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2R87"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:2R85"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 193..206
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 242..259
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:2R85"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:2R85"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:2R85"
SQ SEQUENCE 334 AA; 38298 MW; 78802D9AB5184900 CRC64;
MKVRIATYAS HSALQILKGA KDEGFETIAF GSSKVKPLYT KYFPVADYFI EEKYPEEELL
NLNAVVVPTG SFVAHLGIEL VENMKVPYFG NKRVLRWESD RNLERKWLKK AGIRVPEVYE
DPDDIEKPVI VKPHGAKGGK GYFLAKDPED FWRKAEKFLG IKRKEDLKNI QIQEYVLGVP
VYPHYFYSKV REELELMSID RRYESNVDAI GRIPAKDQLE FDMDITYTVI GNIPIVLRES
LLMDVIEAGE RVVKAAEELM GGLWGPFCLE GVFTPDLEFV VFEISARIVA GTNIFVNGSP
YTWLRYDRPV STGRRIAMEI REAIENDMLE KVLT
