PUR6_YEAST
ID PUR6_YEAST Reviewed; 571 AA.
AC P21264; D6W2I6;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE EC=4.1.1.21;
DE AltName: Full=AIR carboxylase;
DE Short=AIRC;
GN Name=ADE2; OrderedLocusNames=YOR128C; ORFNames=O3293, YOR3293C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2253890; DOI=10.1016/0378-1119(90)90418-q;
RA Stotz A., Linder P.;
RT "The ADE2 gene from Saccharomyces cerevisiae: sequence and new vectors.";
RL Gene 95:91-98(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1514324; DOI=10.1002/yea.320080403;
RA Sasnauskas K., Jomantiene R., Lebediene E., Lebedys J., Januska A.,
RA Janulaitis A.;
RT "Molecular cloning and analysis of autonomous replicating sequence of
RT Candida maltosa.";
RL Yeast 8:253-259(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 -!- MISCELLANEOUS: Present with 5410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; M59824; AAA34401.1; -; Genomic_DNA.
DR EMBL; M58324; AAA34407.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62125.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64047.1; -; Genomic_DNA.
DR EMBL; Z75036; CAA99327.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10902.1; -; Genomic_DNA.
DR PIR; JN0098; DEBYP.
DR RefSeq; NP_014771.3; NM_001183547.3.
DR AlphaFoldDB; P21264; -.
DR SMR; P21264; -.
DR BioGRID; 34523; 99.
DR DIP; DIP-1171N; -.
DR IntAct; P21264; 11.
DR MINT; P21264; -.
DR STRING; 4932.YOR128C; -.
DR iPTMnet; P21264; -.
DR MaxQB; P21264; -.
DR PaxDb; P21264; -.
DR PRIDE; P21264; -.
DR TopDownProteomics; P21264; -.
DR EnsemblFungi; YOR128C_mRNA; YOR128C; YOR128C.
DR GeneID; 854295; -.
DR KEGG; sce:YOR128C; -.
DR SGD; S000005654; ADE2.
DR VEuPathDB; FungiDB:YOR128C; -.
DR eggNOG; KOG2835; Eukaryota.
DR HOGENOM; CLU_011534_2_1_1; -.
DR InParanoid; P21264; -.
DR OMA; ITFDHEH; -.
DR BioCyc; MetaCyc:YOR128C-MON; -.
DR BioCyc; YEAST:YOR128C-MON; -.
DR BRENDA; 4.1.1.21; 984.
DR UniPathway; UPA00074; UER00130.
DR PHI-base; PHI:501; -.
DR PRO; PR:P21264; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P21264; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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; IMP:SGD.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IC:SGD.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IMP:SGD.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IC:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Decarboxylase; Lyase; Nucleotide-binding; Phosphoprotein;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..571
FT /note="Phosphoribosylaminoimidazole carboxylase"
FT /id="PRO_0000075028"
FT DOMAIN 110..298
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 138..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 101
FT /note="R -> G (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> G (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="S -> F (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..253
FT /note="ENAIKSFPGCGIF -> KMQSNFSRLWYI (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="I -> L (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="I -> V (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="P -> T (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="V -> L (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="I -> T (in Ref. 2; AAA34407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 62339 MW; 62D2693916F97AA0 CRC64;
MDSRTVGILG GGQLGRMIVE AANRLNIKTV ILDAENSPAK QISNSNDHVN GSFSNPLDIE
KLAEKCDVLT IEIEHVDVPT LKNLQVKHPK LKIYPSPETI RLIQDKYIQK EHLIKNGIAV
TQSVPVEQAS ETSLLNVGRD LGFPFVLKSR TLAYDGRGNF VVKNKEMIPE ALEVLKDRPL
YAEKWAPFTK ELAVMIVRSV NGLVFSYPIV ETIHKDNICD LCYAPARVPD SVQLKAKLLA
ENAIKSFPGC GIFGVEMFYL ETGELLINEI APRPHNSGHY TIDACVTSQF EAHLRSILDL
PMPKNFTSFS TITTNAIMLN VLGDKHTKDK ELETCERALA TPGSSVYLYG KESRPNRKVG
HINIIASSMA ECEQRLNYIT GRTDIPIKIS VAQKLDLEAM VKPLVGIIMG SDSDLPVMSA
ACAVLKDFGV PFEVTIVSAH RTPHRMSAYA ISASKRGIKT IIAGAGGAAH LPGMVAAMTP
LPVIGVPVKG SCLDGVDSLH SIVQMPRGVP VATVAINNST NAALLAVRLL GAYDSSYTTK
MEQFLLKQEE EVLVKAQKLE TVGYEAYLEN K
