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
//
