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Database: UniProt
Entry: A5UMR4_METS3
LinkDB: A5UMR4_METS3
Original site: A5UMR4_METS3 
ID   A5UMR4_METS3            Unreviewed;       339 AA.
AC   A5UMR4;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE            Short=N5-CAIR mutase {ECO:0000256|HAMAP-Rule:MF_01929};
DE            EC=5.4.99.18 {ECO:0000256|HAMAP-Rule:MF_01929};
DE   AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000256|HAMAP-Rule:MF_01929};
GN   Name=purE {ECO:0000256|HAMAP-Rule:MF_01929};
GN   OrderedLocusNames=Msm_1287 {ECO:0000313|EMBL:ABQ87492.1};
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ87492.1, ECO:0000313|Proteomes:UP000001992};
RN   [1] {ECO:0000313|EMBL:ABQ87492.1, ECO:0000313|Proteomes:UP000001992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC   {ECO:0000313|Proteomes:UP000001992};
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole
CC       ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide
CC       (CAIR). {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01929}.
CC   -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01929}.
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DR   EMBL; CP000678; ABQ87492.1; -; Genomic_DNA.
DR   RefSeq; WP_011954411.1; NZ_CP117965.1.
DR   AlphaFoldDB; A5UMR4; -.
DR   STRING; 420247.Msm_1287; -.
DR   EnsemblBacteria; ABQ87492; ABQ87492; Msm_1287.
DR   GeneID; 78817940; -.
DR   KEGG; msi:Msm_1287; -.
DR   PATRIC; fig|420247.28.peg.1285; -.
DR   eggNOG; arCOG02464; Archaea.
DR   HOGENOM; CLU_782152_0_0_2; -.
DR   UniPathway; UPA00074; UER00943.
DR   Proteomes; UP000001992; Chromosome.
DR   GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1970; -; 2.
DR   HAMAP; MF_01929; PurE_classI; 1.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR024694; PurE_prokaryotes.
DR   NCBIfam; TIGR01162; purE; 1.
DR   PANTHER; PTHR23046:SF2; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1.
DR   PANTHER; PTHR23046; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00731; AIRC; 2.
DR   SMART; SM01001; AIRC; 2.
DR   SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 2.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01929};
KW   Lyase {ECO:0000313|EMBL:ABQ87492.1};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01929}.
FT   DOMAIN          3..151
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   DOMAIN          195..339
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01929"
SQ   SEQUENCE   339 AA;  36736 MW;  F1118363131A3469 CRC64;
     MTPKVMIILG SGSDIAIAEK SMKILEKLEI PYSLKIASAH RTPDLVRELV VQGTNAGIKV
     FIGIAGLAAH LPGAIAAYTH KPVIGVPVDV KVSGLDALYS SVQMPYPSPV ATVGIDRGDN
     GAILAAQILG LYDEEIRKKV LELKEEYKQK VIKNNEEIVQ KIDNPHITND FLRIKNLELN
     ETTEEFNGSY INKNAEVVII VGRHTDLITG KKVSVTLDRL KIPHDMQVIC PIRSGKKFRA
     YVNTMKNAKI FIGINSNSSQ VSGGLVGLTE KPVIGVPCEN ELGNNYLLST VNMPPGVPVA
     TVGVNNGRNA AVLSGEILSI NNPVLLELLE KLKNKKINI
//
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