PUR6_SCHPO
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 03-AUG-2022, entry version 170.
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}.
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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_001023131.2.
DR AlphaFoldDB; P15567; -.
DR SMR; P15567; -.
DR BioGRID; 275318; 11.
DR STRING; 4896.SPCC1322.13.1; -.
DR MaxQB; P15567; -.
DR PaxDb; P15567; -.
DR PRIDE; P15567; -.
DR EnsemblFungi; SPCC1322.13.1; SPCC1322.13.1:pep; SPCC1322.13.
DR GeneID; 2538734; -.
DR KEGG; spo:SPCC1322.13; -.
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: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; TAS:PomBase.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:PomBase.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; ISO:PomBase.
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;
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
