PURE_THEMA
ID PURE_THEMA Reviewed; 171 AA.
AC Q9WYS7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=TM_0446;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-171, AND SUBUNIT.
RX PubMed=15048837; DOI=10.1002/prot.20023;
RA Schwarzenbacher R., Jaroszewski L., von Delft F., Abdubek P., Ambing E.,
RA Biorac T., Brinen L.S., Canaves J.M., Cambell J., Chiu H.-J., Dai X.,
RA Deacon A.M., DiDonato M., Elsliger M.-A., Eshagi S., Floyd R., Godzik A.,
RA Grittini C., Grzechnik S.K., Hampton E., Karlak C., Klock H.E., Koesema E.,
RA Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., Levin I., McMullan D.,
RA McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R.,
RA Quijano K., Robb A., Spraggon G., Stevens R.C., van den Bedem H.,
RA Velasquez J., Vincent J., Wang X., West B., Wolf G., Xu Q., Hodgson K.O.,
RA Wooley J., Wilson I.A.;
RT "Crystal structure of a phosphoribosylaminoimidazole mutase PurE (TM0446)
RT from Thermotoga maritima at 1.77-A resolution.";
RL Proteins 55:474-478(2004).
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}.
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DR EMBL; AE000512; AAD35541.1; -; Genomic_DNA.
DR PIR; G72374; G72374.
DR RefSeq; NP_228256.1; NC_000853.1.
DR RefSeq; WP_004081520.1; NZ_CP011107.1.
DR PDB; 1O4V; X-ray; 1.77 A; A=2-171.
DR PDBsum; 1O4V; -.
DR AlphaFoldDB; Q9WYS7; -.
DR SMR; Q9WYS7; -.
DR STRING; 243274.THEMA_02495; -.
DR EnsemblBacteria; AAD35541; AAD35541; TM_0446.
DR KEGG; tma:TM0446; -.
DR eggNOG; COG0041; Bacteria.
DR InParanoid; Q9WYS7; -.
DR OMA; SNSIDGW; -.
DR OrthoDB; 1701464at2; -.
DR UniPathway; UPA00074; UER00943.
DR EvolutionaryTrace; Q9WYS7; -.
DR Proteomes; UP000008183; 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..171
FT /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT /id="PRO_0000074980"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 13
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1O4V"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1O4V"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1O4V"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1O4V"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1O4V"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1O4V"
FT TURN 52..56
FT /evidence="ECO:0007829|PDB:1O4V"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:1O4V"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1O4V"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1O4V"
FT TURN 90..94
FT /evidence="ECO:0007829|PDB:1O4V"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:1O4V"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:1O4V"
FT HELIX 134..169
FT /evidence="ECO:0007829|PDB:1O4V"
SQ SEQUENCE 171 AA; 18618 MW; 84A995A2E29B8E5F CRC64;
MPRVGIIMGS DSDLPVMKQA AEILEEFGID YEITIVSAHR TPDRMFEYAK NAEERGIEVI
IAGAGGAAHL PGMVASITHL PVIGVPVKTS TLNGLDSLFS IVQMPGGVPV ATVAINNAKN
AGILAASILG IKYPEIARKV KEYKERMKRE VLEKAQRLEQ IGYKEYLNQK E
