PURP_METTH
ID PURP_METTH Reviewed; 363 AA.
AC O27269;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=MTH_1201;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85690.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85690.1; ALT_INIT; Genomic_DNA.
DR PIR; D69027; D69027.
DR RefSeq; WP_048060989.1; NC_000916.1.
DR AlphaFoldDB; O27269; -.
DR SMR; O27269; -.
DR STRING; 187420.MTH_1201; -.
DR EnsemblBacteria; AAB85690; AAB85690; MTH_1201.
DR GeneID; 1471609; -.
DR KEGG; mth:MTH_1201; -.
DR PATRIC; fig|187420.15.peg.1179; -.
DR HOGENOM; CLU_065084_0_0_2; -.
DR OMA; CIHYFYS; -.
DR UniPathway; UPA00074; UER00134.
DR Proteomes; UP000005223; 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..363
FT /note="5-formaminoimidazole-4-carboxamide-1-(beta)-D-
FT ribofuranosyl 5'-monophosphate synthetase"
FT /id="PRO_0000148027"
FT DOMAIN 118..350
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 29
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 96
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 148..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 260
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 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01163"
SQ SEQUENCE 363 AA; 41253 MW; A89014376E6A084A CRC64;
MSKVNRDEIL DILEGYSRED ITVATLGSHT SLHILNGAKQ EGFKTAVVCE KGREVPYQRF
RVADEFIMVD KFSDIVNDDV QDELRSMNSI IVPHGSFVAY AGLDHIENDF YVPMFGNRDI
LRWESERDLE RKLMEEAGIR IPFKYTDPEE IDRTVMVKFP GARGGRGYFV ASSTEEFNEK
IDSMLERGWI TEDDVKDAHI EEYIAGTNFC IHYFYSIMND EVELMGMDSR FESNIDGLVR
IPARDQLDIN LDPSYVITGN HPVAMRESLL PQAFDMGDRM VEAASKIVPP GMNGPFCLQT
MCTDNLEIVT FEMSARTDGG TNTFMHGSTY SYLLHGEGMS MGRRVAREIR VAAEQDRLPE
IIT
