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Database: UniProt
Entry: A5UKI3
LinkDB: A5UKI3
Original site: A5UKI3 
ID   PURP_METS3              Reviewed;         363 AA.
AC   A5UKI3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   16-JAN-2019, entry version 65.
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=Msm_0506;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 /
OS   PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M.,
RA   Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K.,
RA   Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to
RT   the human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86711.1; -; Genomic_DNA.
DR   RefSeq; WP_004036716.1; NC_009515.1.
DR   ProteinModelPortal; A5UKI3; -.
DR   SMR; A5UKI3; -.
DR   STRING; 420247.Msm_0506; -.
DR   EnsemblBacteria; ABQ86711; ABQ86711; Msm_0506.
DR   GeneID; 5216345; -.
DR   KEGG; msi:Msm_0506; -.
DR   PATRIC; fig|420247.28.peg.505; -.
DR   eggNOG; arCOG04346; Archaea.
DR   eggNOG; COG1759; LUCA.
DR   HOGENOM; HOG000228474; -.
DR   KO; K06863; -.
DR   OMA; KFPGARG; -.
DR   UniPathway; UPA00074; UER00134.
DR   Proteomes; UP000001992; 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    363       5-formaminoimidazole-4-carboxamide-1-
FT                                (beta)-D-ribofuranosyl 5'-monophosphate
FT                                synthetase.
FT                                /FTId=PRO_0000348618.
FT   DOMAIN      118    354       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   NP_BIND     148    210       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       299    299       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   METAL       312    312       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING      29     29       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING      96     96       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
FT   BINDING     232    232       ATP. {ECO:0000255|HAMAP-Rule:MF_01163}.
FT   BINDING     260    260       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01163}.
SQ   SEQUENCE   363 AA;  41018 MW;  1B0DD284A59F9C1B CRC64;
     MGEVKLEDIF EILDNYDKDN ITIATLGSHT SLHILQGAKE EGFRTAIVCE KGREVPYQRF
     DVADEYIIVD KFKDIVNEDV QQKLRDMNAI VIPHGSFVAY AGLDNVEDKF NVPMFGNRDI
     LRWEAERDKE RALLVEGEVR IPYKYDNPSE IDRPVMVKFP GARGGRGYFV ASSPEEFNKK
     IDAMKARGWL EDSDVANAHI EEYVSGCNYC IHYFYSALED EVELLGMDTR YESSIDGFVR
     MPAKDQLDID LSPSYVVTGN HPAVIRESLL PQVFEMADKL VESAKKLVAP GLNGPFCMQT
     LVNDNLEVIC FEISARTDGG TNTFMGGSPY SYLTYGKPMS MGRRIALEIK NAIKKEELEK
     IIT
//
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