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Database: UniProt
Entry: A3MTB5
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Original site: A3MTB5 
ID   PURP_PYRCJ              Reviewed;         333 AA.
AC   A3MTB5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   16-JAN-2019, entry version 63.
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};
GN   OrderedLocusNames=Pcal_0449;
OS   Pyrobaculum calidifontis (strain JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C.,
RA   Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP- and formate-dependent formylation of
CC       5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-
CC       monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-
CC       beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of
CC       folates. {ECO:0000255|HAMAP-Rule:MF_01163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC         carboxamide + ATP + formate = 5-formamido-1-(5-phospho-D-
CC         ribosyl)imidazole-4-carboxamide + ADP + phosphate;
CC         Xref=Rhea:RHEA:24836, ChEBI:CHEBI:15740, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58467, ChEBI:CHEBI:58475,
CC         ChEBI:CHEBI:456216; EC=6.3.4.23; Evidence={ECO:0000255|HAMAP-
CC         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;
CC       5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01163}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01163}.
DR   EMBL; CP000561; ABO07882.1; -; Genomic_DNA.
DR   ProteinModelPortal; A3MTB5; -.
DR   SMR; A3MTB5; -.
DR   STRING; 410359.Pcal_0449; -.
DR   EnsemblBacteria; ABO07882; ABO07882; Pcal_0449.
DR   KEGG; pcl:Pcal_0449; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   KO; K06863; -.
DR   OMA; KFPGARG; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000001431; 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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    333       5-formaminoimidazole-4-carboxamide-1-
FT                                (beta)-D-ribofuranosyl 5'-monophosphate
FT                                synthetase.
FT                                /FTId=PRO_0000348633.
FT   DOMAIN      118    313       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   NP_BIND     141    187       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       268    268       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       281    281       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING      21     21       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING      84     84       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING     209    209       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING     229    229       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
SQ   SEQUENCE   333 AA;  37769 MW;  594E7A565AD552E0 CRC64;
     MSAALKRYDL DKLAVATVAS HTALQILRGA KRYGFRTIAV AQRNADFYRQ FSFIDEVWTA
     DFSNFRHVAE KLVEKNALFI PHGSYVEYVG WRQALEAPVP TLGCRELLRW EADQYKKMEL
     LAAAGIPTPR YYKRAEEAEG PVIVKLFGAK GGRGYFVAKN REELAKRIKA VEGDYIIQEY
     VFGVPAYYHY FASPVYNRVE IFGMDIRYET NVDGRTFGWV EPTFVVVGNL PLVLRESLLP
     VVHKYGVDFA KAVREKVSCE LAGPYCLESI IRDDMTIVVF EFSGRIVAGT NVYMGVGSPY
     SVLYFDEPMD MGERIAHEIK EAAARGILEK LFT
//
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