PURE_PYRAB
ID PURE_PYRAB Reviewed; 174 AA.
AC Q9UY68; G8ZJZ4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=PYRAB16400;
GN ORFNames=PAB1077;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50544.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71101.1; -; Genomic_DNA.
DR PIR; B75013; B75013.
DR AlphaFoldDB; Q9UY68; -.
DR SMR; Q9UY68; -.
DR STRING; 272844.PAB1077; -.
DR EnsemblBacteria; CAB50544; CAB50544; PAB1077.
DR KEGG; pab:PAB1077; -.
DR PATRIC; fig|272844.11.peg.1749; -.
DR eggNOG; arCOG02464; Archaea.
DR HOGENOM; CLU_094982_2_0_2; -.
DR OMA; SNSIDGW; -.
DR PhylomeDB; Q9UY68; -.
DR UniPathway; UPA00074; UER00943.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW Isomerase; Purine biosynthesis.
FT CHAIN 1..174
FT /note="N5-carboxyaminoimidazole ribonucleotide mutase"
FT /id="PRO_0000074988"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01929"
SQ SEQUENCE 174 AA; 19000 MW; 5A37D37C0EC7FD01 CRC64;
MVKVGMPKVG IIMGSDSDLP VMKEAAKVLE DFEVDYEMKV ISAHRTPERL HEYARTAEER
GIEVIIAGAG GAAHLPGVLA ALTMIPVIGV PIKSKALNGL DSLLSIVQMP PGIPVATVGI
DGAKNAALLA LEILSIKYPE IKEKLKKYRE DMKRKVEEKS KKLEELGWRK YLEG
