PUR6_CRYNH
ID PUR6_CRYNH Reviewed; 582 AA.
AC P0C017; J9VMR3; O93936; Q92233;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE EC=4.1.1.21;
DE AltName: Full=AIR carboxylase;
DE Short=AIRC;
GN Name=ADE2; ORFNames=CNAG_02294;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RA Perfect J.R.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB09711.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U70673; AAB09711.1; ALT_INIT; mRNA.
DR EMBL; CP003825; AFR95533.1; -; Genomic_DNA.
DR RefSeq; XP_012050060.1; XM_012194670.1.
DR AlphaFoldDB; P0C017; -.
DR SMR; P0C017; -.
DR EnsemblFungi; AFR95533; AFR95533; CNAG_02294.
DR GeneID; 23885928; -.
DR VEuPathDB; FungiDB:CNAG_02294; -.
DR HOGENOM; CLU_011534_2_1_1; -.
DR UniPathway; UPA00074; UER00130.
DR PHI-base; PHI:14; -.
DR Proteomes; UP000010091; Chromosome 6.
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 2: Evidence at transcript level;
KW ATP-binding; Decarboxylase; Lyase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..582
FT /note="Phosphoribosylaminoimidazole carboxylase"
FT /id="PRO_0000075024"
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; 62429 MW; 2AC692442FAF1F7D CRC64;
MAPRKTVGIL GGGQLGRMLT HPAALLGIPL LILDSGSFTP AKQTLLPPPS HSHPDGPFTS
EPHIRKLASA CDILTVEIEH VNADVLEAVE KEGLCEVQPS PKTIRLIQNK YDQKKYLAEK
GVAVAPFEEL PANPTEEDFK AIAGRLGLPL MLKAKTLAYD GRGNSPLKST SSEDIQASLK
FLGDRPLYAE GWAPFVKEVA VMVVRNKEGE VQSYDAVETI HRESILRVCL APLRGERGVN
QRARELAEKA VGHLEGAGIF GVEMFLMPDG ELLLNEIAPR PHNSGHHTIE ACLTSQFENH
LRAILSLPLG STALRVPSAA MVNILGASST MDAIDKMADN ALTVPGAAVH LYGKAESRKA
RKMGHITVTA ESDAELNERL RTLLFAQPDA HADWIDLIAP PSPAPAHSHP KPLVGIIMGS
DSDLPVMHPA TKILEKFGVP YELTITSAHR TPERMVKYAK TAAGRGLRAI IAGAGGAAHL
PGMVASETSL PVIGVPVKAS VLDGVDSLYS IVQMPRGIPC ATVGINNSTN AALLAIRILG
TSVPALNKAT EEYSKALEEE VLAKVDILEE EGWDKYIERL KK
