ID   PUR6_OGAME              Reviewed;         543 AA.
AC   Q01930;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE            EC=4.1.1.21;
DE   AltName: Full=AIR carboxylase;
DE            Short=AIRC;
GN   Name=ADE1;
OS   Ogataea methanolica (Yeast) (Pichia methanolica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=1156966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8109174; DOI=10.1002/yea.320091112;
RA   Hiep T.T., Kulikov V.N., Noskov V.N., Sizonenko G.I., Chernoff Y.O.,
RA   Pavlov Y.I.;
RT   "The 5-aminoimidazole ribonucleotide-carboxylase structural gene of the
RT   methylotrophic yeast Pichia methanolica: cloning, sequencing and homology
RT   analysis.";
RL   Yeast 9:1251-1258(1993).
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; X76529; CAA54041.1; -; Genomic_DNA.
DR   PIR; S39112; S39112.
DR   AlphaFoldDB; Q01930; -.
DR   SMR; Q01930; -.
DR   BRENDA; 4.1.1.21; 7013.
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..543
FT                   /note="Phosphoribosylaminoimidazole carboxylase"
FT                   /id="PRO_0000075025"
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"
SQ   SEQUENCE   543 AA;  58544 MW;  852AADBB8B60EFA3 CRC64;
     MDSQTVGILG GGQLGRMIVE AAHRLNIKTV ILENGDQAPA KQINALDDHI DGSFNDPKAI
     AELAAKCDVL TVEIEHVDTD ALVEVQKATG IKIFPSPETI SLIKDKYLQK EHLIKNGIAV
     AESCSVESSA ASLEEVGAKY GFPYMLKSRT MAYDGRGNFV VKDKSYIPEA LKVLDDRPLY
     AEKWAPFSKE LAVMVVRSID GQVYSYPTVE TIHQNNICHT VFAPARVNDT VQKKAQILAD
     NAVKSFPGAG IFGVEMFLLQ NGDLLVNEIA PRPHNSGHYT IDACVTSQFE AHVRAITGLP
     MPKNFTCLST PSTQAIMLNV LGGDEQNGEF KMCKRALETP HASVYLYGKT TRPGRKMGHI
     NIVSQSMTDC ERRLHYIEGT TNSIPLEEQY TTDSIPGTSS KPLVGVIMGS DSDLPVMSLG
     CNILKQFNVP FEVTIVSAHR TPQRMAKYAI DAPKRGLKCI IAGAGGAAHL PGMVAAMTPL
     PVIGVPVKGS TLDGVDSLHS IVQMPRGIPV ATVAINNATN AALLAITILG AGDPNTCLQW
     KFI