PURP_METBU
ID PURP_METBU Reviewed; 355 AA.
AC Q12VJ6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Mbur_1626;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE52530.1; -; Genomic_DNA.
DR RefSeq; WP_011499674.1; NC_007955.1.
DR AlphaFoldDB; Q12VJ6; -.
DR SMR; Q12VJ6; -.
DR STRING; 259564.Mbur_1626; -.
DR PRIDE; Q12VJ6; -.
DR EnsemblBacteria; ABE52530; ABE52530; Mbur_1626.
DR GeneID; 3997260; -.
DR KEGG; mbu:Mbur_1626; -.
DR HOGENOM; CLU_065084_0_0_2; -.
DR OMA; CIHYFYS; -.
DR OrthoDB; 21169at2157; -.
DR UniPathway; UPA00074; UER00134.
DR Proteomes; UP000001979; 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; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..355
FT /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT ribofuranosyl 5'-monophosphate synthetase"
FT /id="PRO_0000348619"
FT DOMAIN 101..332
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 144..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 254
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 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
SQ SEQUENCE 355 AA; 39911 MW; 719D64ABDF759C72 CRC64;
MISKQQISEI ISNYDLNDLA IATVCSHSSL QIFDGARKEG LRTIGICVGQ PPRFYDAFPK
AKPDEYIVVE SYSDIPKIAE ELVRKNAIVI PHGSFVEYMG TESFAELAVP TFGNREVLEW
ESDRDKEREW LEGAGIHMPK IVDPEKIESP VMVKYHGAKG GRGFFIAKDY EEFKQYIDPN
EKHTVQEFIV GTRYYLHFFY SPIREEGYKL SEGILEMLSM DRRVESNADE IFRLGSPKEL
EDAGIHPTYV VTGNVPLVAR ESLLPRIFAL GEKVVEESLG LFGGMIGPFC LETVFTDKLE
IKVFEISARI VAGTNLYTSG SPYSDMIEEN LSTGKRIAQE IKLGAKTGKL DLILS
