PURE_METJA
ID PURE_METJA Reviewed; 157 AA.
AC Q58033;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929};
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=MJ0616;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB98611.1; -; Genomic_DNA.
DR PIR; H64376; H64376.
DR RefSeq; WP_010870121.1; NC_000909.1.
DR PDB; 2YWX; X-ray; 2.31 A; A=1-157.
DR PDBsum; 2YWX; -.
DR AlphaFoldDB; Q58033; -.
DR SMR; Q58033; -.
DR STRING; 243232.MJ_0616; -.
DR PRIDE; Q58033; -.
DR EnsemblBacteria; AAB98611; AAB98611; MJ_0616.
DR GeneID; 1451482; -.
DR KEGG; mja:MJ_0616; -.
DR eggNOG; arCOG02464; Archaea.
DR HOGENOM; CLU_094982_2_0_2; -.
DR InParanoid; Q58033; -.
DR OMA; SNSIDGW; -.
DR OrthoDB; 104083at2157; -.
DR PhylomeDB; Q58033; -.
DR UniPathway; UPA00074; UER00943.
DR EvolutionaryTrace; Q58033; -.
DR Proteomes; UP000000805; 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; 1.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR Pfam; PF00731; AIRC; 1.
DR PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
DR TIGRFAMs; TIGR01162; purE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..157
FT /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT /id="PRO_0000074987"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:2YWX"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2YWX"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:2YWX"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:2YWX"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:2YWX"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2YWX"
FT HELIX 128..153
FT /evidence="ECO:0007829|PDB:2YWX"
SQ SEQUENCE 157 AA; 16951 MW; 398E2DDA35030078 CRC64;
MICIIMGSES DLKIAEKAVN ILKEFGVEFE VRVASAHRTP ELVEEIVKNS KADVFIAIAG
LAAHLPGVVA SLTTKPVIAV PVDAKLDGLD ALLSSVQMPP GIPVATVGID RGENAAILAL
EILALKDENI AKKLIEYREK MKKKVYASDE KVKEMFK
