PURE_ARCFU
ID PURE_ARCFU Reviewed; 180 AA.
AC O28997;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000255|HAMAP-Rule:MF_02045};
DE EC=4.1.1.21 {ECO:0000255|HAMAP-Rule:MF_02045};
DE AltName: Full=AIR carboxylase {ECO:0000255|HAMAP-Rule:MF_02045};
DE Short=AIRC {ECO:0000255|HAMAP-Rule:MF_02045};
GN Name=purE {ECO:0000255|HAMAP-Rule:MF_02045}; OrderedLocusNames=AF_1271;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Catalyzes the reversible conversion of 5-aminoimidazole
CC ribonucleotide (AIR) and CO(2) to 4-carboxy-5-aminoimidazole
CC ribonucleotide (CAIR). {ECO:0000255|HAMAP-Rule:MF_02045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+)
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02045};
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 (carboxylase route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_02045}.
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02045}.
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DR EMBL; AE000782; AAB89973.1; -; Genomic_DNA.
DR PIR; F69408; F69408.
DR AlphaFoldDB; O28997; -.
DR SMR; O28997; -.
DR STRING; 224325.AF_1271; -.
DR EnsemblBacteria; AAB89973; AAB89973; AF_1271.
DR KEGG; afu:AF_1271; -.
DR eggNOG; arCOG02464; Archaea.
DR HOGENOM; CLU_094982_2_0_2; -.
DR OMA; TKPVIAC; -.
DR PhylomeDB; O28997; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02045; PurE_classII; 1.
DR InterPro; IPR033626; PurE_classII.
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 Lyase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..180
FT /note="Phosphoribosylaminoimidazole carboxylase"
FT /id="PRO_0000074986"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045"
SQ SEQUENCE 180 AA; 20015 MW; 81F6152E6E14D69D CRC64;
MSQFLSLRNC LRLTIRLLRQ FRRGEGMKAV IIMGSKSDLD YSKKIASKLA DFGIDAVMRI
ASAHKTPEKV LEIIKEYEKE DVVFVTVAGR SNALSGFVDA NTSKPVIASP PYSDKFGGAD
IFSSIRMPSG VAPMLVLEAE NAALAVAKIF ALKDEGVREK VVQFQENKRR EIYKADEELR
