ID   PUR6_SCHOC              Reviewed;         557 AA.
AC   P50504;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE            EC=4.1.1.21;
DE   AltName: Full=AIR carboxylase;
DE            Short=AIRC;
GN   Name=ADE2;
OS   Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Schwanniomyces.
OX   NCBI_TaxID=27300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8553700; DOI=10.1002/yea.320111309;
RA   Gourdon P., Janatova I., Meilhoc E., Klein R.D., Costaglioli P.,
RA   Masson J.-M.;
RT   "Sequence analysis of the ADE2 gene coding for phosphoribosylaminoimidazole
RT   carboxylase in Schwanniomyces occidentalis.";
RL   Yeast 11:1289-1293(1995).
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; U23210; AAA96380.1; -; Genomic_DNA.
DR   PIR; S60392; S60392.
DR   AlphaFoldDB; P50504; -.
DR   SMR; P50504; -.
DR   PRIDE; P50504; -.
DR   UniPathway; UPA00074; UER00130.
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..557
FT                   /note="Phosphoribosylaminoimidazole carboxylase"
FT                   /id="PRO_0000075026"
FT   DOMAIN          108..296
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         136..191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   557 AA;  61338 MW;  EE5338090FC2E41A CRC64;
     MDNKIVGILG GGQLGRMIVE AANRLNIKTV VLDVPNSPAK QINSNEHVDG SFTDLKSIIQ
     LAEKCDILTV EIEHVDVEAL KYVKEKFGVE IYPLPDTIKL IQDKYLQKEH LIQHGISVTE
     SVAVPSNDEQ SLIEIGNKFN YPFMLKSRTL AYDGRGNYVV KTKESIPEAL EFLKDRPLYA
     EKWCPFNKEL AVMVVRSIEG EVFAYPTVET IHKNNICHVV YAPARVSDSI AVKASVLAKN
     AVKSFPGCGI FGVEMFLLPN NEILINEIAP RPHNSGHYTI DACVTSQFEA HVRAVVGLPM
     PKNFTSLSTT TTNAIMLNVL GDEESNKELE ICRRALETPN ASVYLYGKST RPNRKMGHIN
     IVSSSMEDCE SRLDYIIGKS SKIPENLIPK EKPLVSIIMG SDSDLPVMSV GANILKRFGV
     PFELTIVSAH RTPHRMTQYA IEAPKRGLKV IIAGAGGAAH LPGMVAAMTP LPVIGVPVKG
     STLDGVDSLH SIVQMPRGIP VATVAINNST NAALLAVRIL GAYDYKWLNE MNQYMNNMEN
     EVLAKAERLE EVGYEKY