ID   PUR6_CANGA              Reviewed;         570 AA.
AC   O74197; Q6FM75;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE            EC=4.1.1.21 {ECO:0000305|PubMed:9602176};
DE   AltName: Full=AIR carboxylase;
DE            Short=AIRC;
GN   Name=ADE2; OrderedLocusNames=CAGL0K10340g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=9602176; DOI=10.1016/s0378-1119(98)00157-7;
RA   Hanic-Joyce P.J., Joyce P.B.M.;
RT   "A high-copy-number ADE2-bearing plasmid for transformation of Candida
RT   glabrata.";
RL   Gene 211:395-400(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:0000305|PubMed:9602176};
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   -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC       family. Class I subfamily. {ECO:0000305}.
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DR   EMBL; AF030388; AAC27548.1; -; Genomic_DNA.
DR   EMBL; CR380957; CAG61632.1; -; Genomic_DNA.
DR   RefSeq; XP_448669.1; XM_448669.1.
DR   AlphaFoldDB; O74197; -.
DR   SMR; O74197; -.
DR   STRING; 5478.XP_448669.1; -.
DR   EnsemblFungi; CAG61632; CAG61632; CAGL0K10340g.
DR   GeneID; 2890129; -.
DR   KEGG; cgr:CAGL0K10340g; -.
DR   CGD; CAL0134467; ADE2.
DR   VEuPathDB; FungiDB:CAGL0K10340g; -.
DR   eggNOG; KOG2835; Eukaryota.
DR   HOGENOM; CLU_011534_2_1_1; -.
DR   InParanoid; O74197; -.
DR   OMA; ITFDHEH; -.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IGI:CGD.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IGI:CGD.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_01929; PurE_classI; 1.
DR   HAMAP; MF_01928; PurK; 1.
DR   InterPro; IPR016301; Ade2_fungi/plant.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR033747; PurE_ClassI.
DR   InterPro; IPR000031; PurE_dom.
DR   InterPro; IPR005875; PurK.
DR   InterPro; IPR040686; PurK_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF00731; AIRC; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF17769; PurK_C; 1.
DR   PIRSF; PIRSF001340; AIR_carboxylase; 1.
DR   SMART; SM01001; AIRC; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01162; purE; 1.
DR   TIGRFAMs; TIGR01161; purK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Decarboxylase; Lyase; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..570
FT                   /note="Phosphoribosylaminoimidazole carboxylase"
FT                   /id="PRO_0000075022"
FT   DOMAIN          110..297
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         137..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   CONFLICT        477..478
FT                   /note="MT -> IA (in Ref. 1; AAC27548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        491
FT                   /note="T -> F (in Ref. 1; AAC27548)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   570 AA;  62712 MW;  481BA9042F0C532A CRC64;
     MDSRTVGILG GGQLGRMIVE AANRLNIKTL ILDAPNSPAK QITNASDHVD GSFANKEDIE
     ALAAKCDVMT VEIEHVDVNA LKEVQKQFPK LEIYPTPETI GLIQDKYVQK QHLVKNRIPV
     VPSITVENSK ESLIKTGSSL GYPFVLKSRT LAYDGRGNFV VKSEEDIEKG LEFLANRPLY
     AEKWASFKKE LSVMIIRSLD GRVYSYPIVE TIHKNNVCHL CYVPARVPDS VQHKAKLMAE
     NAIKSFPGCG IFGVEMFLLD DDSIVLNEIA PRPHNSGHYT INACVVSQFE AHLRAILDLP
     MPKNFTSLST NSTNAIMLNL LGDPETKDKE LQICERALNT PGASVYLYGK ESKPNRKVGH
     INIVCSSMKE CDKRLQFIMG LKTDPIKHSV MEILNAEEVR KPLVGVIMGS DSDLPVMSAA
     CKMLEQFEVP FEVTIVSAHR TPYRMNKYAS EAVSRGIKVI IAGAGGAAHL PGMVAAMTPV
     PVIGVPVKGS TLDGVDSLHS IVQMPRGVPV ATVAINNSTN AGILAVRMLG IHNYDYVKKM
     EEFLNKQEEE VLQKAAKLES IGYEKYLESK