ID   PUR6_CRYNB              Reviewed;         582 AA.
AC   P0CQ37; 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 55.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE            EC=4.1.1.21;
DE   AltName: Full=AIR carboxylase;
DE            Short=AIRC;
GN   Name=ADE2; OrderedLocusNames=CNBE2520;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B-3501;
RX   PubMed=10413613; DOI=10.1006/fgbi.1999.1126;
RA   Sudarshan S., Davidson R.C., Heitman J., Alspaugh J.A.;
RT   "Molecular analysis of the Cryptococcus neoformans ADE2 gene, a selectable
RT   marker for transformation and gene disruption.";
RL   Fungal Genet. Biol. 27:36-48(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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; AF112302; AAC98316.1; -; Genomic_DNA.
DR   EMBL; AAEY01000024; EAL20891.1; -; Genomic_DNA.
DR   RefSeq; XP_775538.1; XM_770445.1.
DR   AlphaFoldDB; P0CQ37; -.
DR   SMR; P0CQ37; -.
DR   EnsemblFungi; EAL20891; EAL20891; CNBE2520.
DR   GeneID; 4936262; -.
DR   KEGG; cnb:CNBE2520; -.
DR   VEuPathDB; FungiDB:CNBE2520; -.
DR   HOGENOM; CLU_011534_2_1_1; -.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000001435; 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.
FT   CHAIN           1..582
FT                   /note="Phosphoribosylaminoimidazole carboxylase"
FT                   /id="PRO_0000410228"
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;  62447 MW;  5A04D86836FB5250 CRC64;
     MAPRKTVGIL GGGQLGRMLT HPAALLGIPL LILDSGSYTP AKQTLLPPPP HSHPDGPFTS
     ETHIRKLASA CDILTVEIEH VNADVLEAVE KEGLCEVQPS PKTIRLIQNK YDQKKYLAER
     GVAVAPFEEL PANPTEEDFK AIAGRLGLPL MLKAKTLAYD GRGNSPLKSA SSEDIQASLK
     FLGDRPLYAE GWAPFVKEVA VMVVRNKEGE VQSYDAVETI HRESILRVCL TPLRGEKGVN
     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 VLAKVDILEE EGWDKYIERL KK