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PURP_METM6
ID   PURP_METM6              Reviewed;         361 AA.
AC   A9A9U0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=MmarC6_1300;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) 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}.
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DR   EMBL; CP000867; ABX02113.1; -; Genomic_DNA.
DR   RefSeq; WP_012194057.1; NC_009975.1.
DR   AlphaFoldDB; A9A9U0; -.
DR   SMR; A9A9U0; -.
DR   STRING; 444158.MmarC6_1300; -.
DR   EnsemblBacteria; ABX02113; ABX02113; MmarC6_1300.
DR   GeneID; 5737554; -.
DR   KEGG; mmx:MmarC6_1300; -.
DR   eggNOG; arCOG04346; Archaea.
DR   HOGENOM; CLU_065084_0_0_2; -.
DR   OMA; CIHYFYS; -.
DR   OrthoDB; 21169at2157; -.
DR   PhylomeDB; A9A9U0; -.
DR   UniPathway; UPA00074; UER00134.
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.
FT   CHAIN           1..361
FT                   /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT                   ribofuranosyl 5'-monophosphate synthetase"
FT                   /id="PRO_0000348622"
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                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         94
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         146..208
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT   BINDING         258
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         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"
SQ   SEQUENCE   361 AA;  40468 MW;  98D7A8D4AAE405F7 CRC64;
     MIPKEEIMGI FEKYNKDEVT IVTVGSHTSL HILKGAKLEG FSTAVITTRD RDIPYKRFGV
     ADKFIYVDKF SDISKEEIQQ QLRDMNAIIV PHGSFIAYCG LDNVEDTFKV PMFGNRAILR
     WEAERDLEGQ LLGGSGLRIP KKYGGPDDID GPVMVKFPGA RGGRGYFPCS TVEEFWRKIG
     EFKAKGILTE DDVKKAHIEE YVVGANYCIH YFYSPLKDQV ELMGIDRRYE SSIDGLVRVP
     AKDQLELSID PSYVITGNFP VVIRESLLPQ VFDMGDKLAT KAKELVKPGM LGPFCLQSLC
     NENLELVVFE MSARVDGGTN TFMNGSPYSC LYTGEPLSMG QRIAKEIKLA LELKMIDKVI
     S
 
 
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