ID   PUR6_CRYNJ              Reviewed;         582 AA.
AC   P0CQ36; O93936; Q55SD0; Q5KGS6; Q92233;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE            EC=4.1.1.21;
DE   AltName: Full=AIR carboxylase;
DE            Short=AIRC;
GN   Name=ADE2; OrderedLocusNames=CNE02500;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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   -!- 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; AE017345; AAW43646.1; -; Genomic_DNA.
DR   RefSeq; XP_570953.1; XM_570953.1.
DR   AlphaFoldDB; P0CQ36; -.
DR   SMR; P0CQ36; -.
DR   STRING; 5207.AAW43646; -.
DR   PaxDb; P0CQ36; -.
DR   EnsemblFungi; AAW43646; AAW43646; CNE02500.
DR   GeneID; 3257629; -.
DR   KEGG; cne:CNE02500; -.
DR   VEuPathDB; FungiDB:CNE02500; -.
DR   eggNOG; KOG2835; Eukaryota.
DR   HOGENOM; CLU_011534_2_1_1; -.
DR   InParanoid; P0CQ36; -.
DR   OMA; CRAGRKM; -.
DR   OrthoDB; 945274at2759; -.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000002149; Chromosome 5.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   ATP-binding; Decarboxylase; Lyase; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..582
FT                   /note="Phosphoribosylaminoimidazole carboxylase"
FT                   /id="PRO_0000075023"
FT   DOMAIN          114..305
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         143..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   582 AA;  62345 MW;  A2136CC3DAAEB142 CRC64;
     MAPRKTVGIL GGGQLGRMLT HPAALLGIPL LILDSGSYTP AKQTLLPPPP HSHPDGPFTS
     ETHIRKLASA CDILTVEIEH VNADVLEAVE KEGLCEVQPS PQTIRLIQNK YDQKKYLAER
     GVAVAPFEEL PANPTEEDFK AIAGRLGLPL MLKAKTLAYD GRGNSPLKSA SSGDIQASLK
     FLGDRPLYAE GWAPFVKEVA VMVVRNKEGE VRSYDAVETI HRESILRVCL APLRGEKGVN
     QRARELAEKA VGHLEGAGIF GVEMFLMPDG ELLLNEIAPR PHNSGHHTIE ACLTSQFENH
     LRAILSLPLG STALRVPSAA MVNILGASST MDAIDKMADN ALTVPGAAVH LYGKAESRKA
     RKMGHITVTA ESDAELNERL RALLFAQPDA HADWIDLIAP PSPAPAHSHA KPLVGIIMGS
     DSDLPVMHPA TKILEKFGVP YELTITSAHR TPERMVKYAK TAADRGLRAI IAGAGGAAHL
     PGMVASETSL PVIGVPVKAS VLDGVDSLYS IVQMPRGIPC ATVGINNSTN AALLAVRILG
     TSVPALNKAT EEYSKALEEE VLAKADILEE EGWDKYIERL KK