ID   PURE_METTH              Reviewed;         334 AA.
AC   P41654;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000305};
DE            Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929};
DE            EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
GN   Name=purE {ECO:0000255|HAMAP-Rule:MF_01929}; OrderedLocusNames=MTH_1393;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=3936936; DOI=10.1007/bf02115691;
RA   Hamilton P.T., Reeve J.N.;
RT   "Sequence divergence of an archaebacterial gene cloned from a mesophilic
RT   and a thermophilic methanogen.";
RL   J. Mol. Evol. 22:351-360(1985).
RN   [2]
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 conversion of N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC       (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-
CC         amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate;
CC         Xref=Rhea:RHEA:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:58730,
CC         ChEBI:CHEBI:77657; EC=5.4.99.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01929};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01929}.
CC   -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01929}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB85870.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X03250; CAA27010.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB85870.1; ALT_INIT; Genomic_DNA.
DR   PIR; D69052; D69052.
DR   RefSeq; WP_048061041.1; NC_000916.1.
DR   AlphaFoldDB; P41654; -.
DR   SMR; P41654; -.
DR   STRING; 187420.MTH_1393; -.
DR   EnsemblBacteria; AAB85870; AAB85870; MTH_1393.
DR   GeneID; 1471110; -.
DR   KEGG; mth:MTH_1393; -.
DR   PATRIC; fig|187420.15.peg.1358; -.
DR   HOGENOM; CLU_782152_0_0_2; -.
DR   OMA; AHRTHEK; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01929; PurE_classI; 2.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   Pfam; PF00731; AIRC; 2.
DR   SMART; SM01001; AIRC; 2.
DR   TIGRFAMs; TIGR01162; purE; 2.
PE   3: Inferred from homology;
KW   Isomerase; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Probable N5-carboxyaminoimidazole ribonucleotide
FT                   mutase"
FT                   /id="PRO_0000074992"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
SQ   SEQUENCE   334 AA;  36245 MW;  502E0E964ECC7A65 CRC64;
     MKPRVMILLG SASDFRIAEK AMEIFEELRI PYDLRVASAH RTHEKVKAIV SEAVKAGVEV
     FIGIAGLSAH LPGMISANTH RPVIGVPVDV KLGGLDALFA CSQMPFPAPV ATVGVDRGEN
     AAILAAQIIG IGDPGVRERV ADLRRGFYER VRRDECQVLN SIEGSYYAPL EVEMPPIGDK
     VPSDSQDDPM VSVIPGSYSD MKIAKKTTMF LERMGISYDL NVISPIRYPE RFERYLEKME
     NVKLFIAISG LSAHVTGAVV ALSDRPVIGV PCPLKMNGWD SLLSMINMPP GVPVGTVGVG
     NGGNAAILAA EMLGIYDEKI ESRIKRIKSR SVKF