ID PUR6_SCHPO Reviewed; 552 AA. AC P15567; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 02-SEP-2026, entry version 184. DE RecName: Full=Phosphoribosylaminoimidazole carboxylase; DE EC=4.1.1.21; DE AltName: Full=AIR carboxylase; DE Short=AIRC; GN Name=ade6; Synonyms=min1; ORFNames=SPCC1322.13; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3221399; DOI=10.1016/0022-2836(88)90051-4; RA Szankasi P., Heyer W.-D., Schuchert P., Kohli J.; RT "DNA sequence analysis of the ade6 gene of Schizosaccharomyces pombe. Wild- RT type and mutant alleles including the recombination host spot allele ade6- RT M26."; RL J. Mol. Biol. 204:917-925(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M37264; AAA35285.1; -; Genomic_DNA. DR EMBL; X14488; CAA32650.1; -; Genomic_DNA. DR EMBL; CU329672; CAA22866.1; -; Genomic_DNA. DR PIR; S02159; DEZPP. DR RefSeq; NP_588141.1; NM_001023131.3. DR AlphaFoldDB; P15567; -. DR SMR; P15567; -. DR BioGRID; 275318; 11. DR FunCoup; P15567; 89. DR STRING; 284812.P15567; -. DR iPTMnet; P15567; -. DR PaxDb; 284812-P15567; -. DR GeneID; 2538734; -. DR KEGG; spo:2538734; -. DR PomBase; SPCC1322.13; ade6. DR VEuPathDB; FungiDB:SPCC1322.13; -. DR eggNOG; KOG2835; Eukaryota. DR HOGENOM; CLU_011534_2_1_1; -. DR InParanoid; P15567; -. DR OMA; ITFDHEH; -. DR PhylomeDB; P15567; -. DR BRENDA; 4.1.1.21; 5613. DR UniPathway; UPA00074; UER00130. DR PRO; PR:P15567; -. DR Proteomes; UP000002485; Chromosome III. DR GO; GO:0005829; C:cytosol; HDA:PomBase. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:PomBase. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; ISO:PomBase. DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central. DR FunFam; 3.40.50.1970:FF:000013; Phosphoribosylaminoimidazole carboxylase; 1. DR FunFam; 3.40.50.20:FF:000030; Phosphoribosylaminoimidazole carboxylase; 1. DR FunFam; 3.30.470.20:FF:000037; Phosphoribosylaminoimidazole carboxylase, chloroplastic; 1. DR FunFam; 3.30.1490.20:FF:000016; phosphoribosylaminoimidazole carboxylase, chloroplastic; 1. DR Gene3D; 3.40.50.1970; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; IPR054350; PurT/PurK_preATP-grasp. DR InterPro; IPR011054; Rudment_hybrid_motif. DR NCBIfam; NF004679; PRK06019.1-5; 1. DR NCBIfam; TIGR01162; purE; 1. DR NCBIfam; TIGR01161; purK; 1. DR PANTHER; PTHR11609:SF5; PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE; 1. DR PANTHER; PTHR11609; PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7; 1. DR Pfam; PF00731; AIRC; 1. DR Pfam; PF02222; ATP-grasp; 1. DR Pfam; PF17769; PurK_C; 1. DR Pfam; PF22660; RS_preATP-grasp-like; 1. DR PIRSF; PIRSF001340; AIR_carboxylase; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR SUPFAM; SSF51246; Rudiment single hybrid motif; 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..552 FT /note="Phosphoribosylaminoimidazole carboxylase" FT /id="PRO_0000075027" FT DOMAIN 108..295 FT /note="ATP-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" FT BINDING 134..189 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409" SQ SEQUENCE 552 AA; 60013 MW; 2C10AF7C4349808F CRC64; MSEKQVVGIL GGGQLGRMMV EAAHRLNIKC IILDAANSPA KQIDGGREHI DASFTDPDAI VELSKKCTLL TTEIEHINTD ALAAVTKSVA VEPSPATLRC IQDKYLQKQH LQVFKIALPE FCDAPDQESV EKAGQEFGYP FVLKSKTLAY DGRGNYVVHQ PSEIPTAIKA LGDRPLYVEK FVPFSMEIAV MVVRSLDGKV YAYPTTETIQ KDNVCHLVYA PARLPFSIQQ RAQTLAMDAV RTFEGAGIYG VEMFVLQDGE TILLNEIAPR PHNSGHYTIE ACPTSQFEAH LRAICGLPFS EINTQLSTST THALMVNILG TDDPDYVSKI AKRSLSIPGA TLHLYGKAES RKGRKMGHVT IISDSPQECE RRYQMLLDVK DPVESPVVGI IMGSDSDLSK MKDAAVILDE FKVPYELTIV SAHRTPDRMV TYARTAASRG LRVIIAGAGG AAHLPGMVAA MTPLPVIGVP VKGSTLDGVD SLHSIVQMPR GVPVATVAIN NSQNAGILAC RILATFQPSL LAAMESFMDN MKEIVLEKAD KLEKVGWKNY SA //