PURP_METJA
ID PURP_METJA Reviewed; 361 AA.
AC Q57600;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=MJ0136;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15623504; DOI=10.1074/jbc.m413937200;
RA Ownby K., Xu H., White R.H.;
RT "A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-
RT formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate
RT synthetase: a new enzyme in purine biosynthesis.";
RL J. Biol. Chem. 280:10881-10887(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 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, ECO:0000269|PubMed:15623504}.
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;
CC Evidence={ECO:0000269|PubMed:15623504};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15623504};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000269|PubMed:15623504};
CC -!- ACTIVITY REGULATION: Inhibited by ADP. {ECO:0000269|PubMed:15623504}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.25. {ECO:0000269|PubMed:15623504};
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: Homohexamer. Dimer of trimers. {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; L77117; AAB98117.1; -; Genomic_DNA.
DR PIR; H64316; H64316.
DR RefSeq; WP_010869629.1; NC_000909.1.
DR PDB; 2R7K; X-ray; 2.10 A; A=1-361.
DR PDB; 2R7L; X-ray; 2.10 A; A=1-361.
DR PDB; 2R7M; X-ray; 2.30 A; A=1-361.
DR PDB; 2R7N; X-ray; 2.40 A; A=1-361.
DR PDBsum; 2R7K; -.
DR PDBsum; 2R7L; -.
DR PDBsum; 2R7M; -.
DR PDBsum; 2R7N; -.
DR AlphaFoldDB; Q57600; -.
DR SMR; Q57600; -.
DR STRING; 243232.MJ_0136; -.
DR PRIDE; Q57600; -.
DR EnsemblBacteria; AAB98117; AAB98117; MJ_0136.
DR GeneID; 1450977; -.
DR KEGG; mja:MJ_0136; -.
DR eggNOG; arCOG04346; Archaea.
DR HOGENOM; CLU_065084_0_0_2; -.
DR InParanoid; Q57600; -.
DR OMA; CIHYFYS; -.
DR OrthoDB; 21169at2157; -.
DR PhylomeDB; Q57600; -.
DR BioCyc; MetaCyc:MON-14616; -.
DR BRENDA; 6.3.4.23; 3260.
DR UniPathway; UPA00074; UER00134.
DR EvolutionaryTrace; Q57600; -.
DR Proteomes; UP000000805; 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..361
FT /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT ribofuranosyl 5'-monophosphate synthetase"
FT /id="PRO_0000148024"
FT DOMAIN 116..348
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 27
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 94
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 156..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 199..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 258
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
FT carboxamide"
FT /ligand_id="ChEBI:CHEBI:58475"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2R7K"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2R7N"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:2R7K"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2R7N"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 204..214
FT /evidence="ECO:0007829|PDB:2R7K"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 219..232
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 268..285
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:2R7K"
FT STRAND 306..315
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 317..322
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:2R7K"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:2R7K"
SQ SEQUENCE 361 AA; 40824 MW; 0B9928DDD41D4DB6 CRC64;
MISKDEILEI FDKYNKDEIT IATLGSHTSL HILKGAKLEG FSTVCITMKG RDVPYKRFKV
ADKFIYVDNF SDIKNEEIQE KLRELNSIVV PHGSFIAYCG LDNVENSFLV PMFGNRRILR
WESERSLEGK LLREAGLRVP KKYESPEDID GTVIVKFPGA RGGRGYFIAS STEEFYKKAE
DLKKRGILTD EDIANAHIEE YVVGTNFCIH YFYSPLKDEV ELLGMDKRYE SNIDGLVRIP
AKDQLEMNIN PSYVITGNIP VVIRESLLPQ VFEMGDKLVA KAKELVPPGM IGPFCLQSLC
NENLELVVFE MSARVDGGTN SFMNGGPYSF LYNGEPLSMG QRIAREIKMA LQLDMIDKII
S
