PUR91_YEAST
ID PUR91_YEAST Reviewed; 591 AA.
AC P54113; D6VY30; E9PAG6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Bifunctional purine biosynthesis protein ADE16;
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE EC=2.1.2.3;
DE AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase;
DE AltName: Full=AICAR transformylase;
DE Includes:
DE RecName: Full=IMP cyclohydrolase;
DE EC=3.5.4.10;
DE AltName: Full=ATIC;
DE AltName: Full=IMP synthase;
DE AltName: Full=Inosinicase;
GN Name=ADE16; OrderedLocusNames=YLR028C;
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].
RA Tibbetts A.S., Appling D.R.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1.
CC -!- SUBUNIT: Homodimer (Possible).
CC -!- INTERACTION:
CC P54113; P38009: ADE17; NbExp=5; IntAct=EBI-14213, EBI-14223;
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 7700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA97551.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; U62402; AAB57774.1; -; Genomic_DNA.
DR EMBL; Z73199; CAA97551.2; ALT_SEQ; Genomic_DNA.
DR EMBL; Z73200; CAA97552.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09346.1; -; Genomic_DNA.
DR PIR; S77707; S77707.
DR RefSeq; NP_013128.1; NM_001181915.1.
DR AlphaFoldDB; P54113; -.
DR SMR; P54113; -.
DR BioGRID; 31302; 182.
DR DIP; DIP-4657N; -.
DR IntAct; P54113; 17.
DR MINT; P54113; -.
DR STRING; 4932.YLR028C; -.
DR CarbonylDB; P54113; -.
DR iPTMnet; P54113; -.
DR MaxQB; P54113; -.
DR PaxDb; P54113; -.
DR PRIDE; P54113; -.
DR TopDownProteomics; P54113; -.
DR EnsemblFungi; YLR028C_mRNA; YLR028C; YLR028C.
DR GeneID; 850715; -.
DR KEGG; sce:YLR028C; -.
DR SGD; S000004018; ADE16.
DR VEuPathDB; FungiDB:YLR028C; -.
DR eggNOG; KOG2555; Eukaryota.
DR GeneTree; ENSGT00390000004553; -.
DR HOGENOM; CLU_016316_3_2_1; -.
DR InParanoid; P54113; -.
DR OMA; EQDRVGC; -.
DR BioCyc; MetaCyc:YLR028C-MON; -.
DR BioCyc; YEAST:YLR028C-MON; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR PRO; PR:P54113; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P54113; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IDA:SGD.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IDA:SGD.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IDA:SGD.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:SGD.
DR Gene3D; 1.10.287.440; -; 1.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_00139; PurH; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692; PTHR11692; 1.
DR Pfam; PF01808; AICARFT_IMPCHas; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..591
FT /note="Bifunctional purine biosynthesis protein ADE16"
FT /id="PRO_0000192159"
FT DOMAIN 1..147
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ SEQUENCE 591 AA; 65282 MW; DEC06684BFED7CA7 CRC64;
MGKYTKTAIL SVYDKTGLLD LAKGLVENNV RILASGGTAN MVREAGFPVD DVSSITHAPE
MLGGRVKTLH PAVHAGILAR NLEGDEKDLK EQHIDKVDFV VCNLYPFKET VAKIGVTVQE
AVEEIDIGGV TLLRAAAKNH SRVTILSDPN DYSIFLQDLS KDGEISQDLR NRFALKAFEH
TADYDAAISD FFRKQYSEGK AQLPLRYGCN PHQRPAQAYI TQQEELPFKV LCGTPGYINL
LDALNSWPLV KELSASLNLP AAASFKHVSP AGAAVGLPLS DVERQVYFVN DMEDLSPLAC
AYARARGADR MSSFGDFIAL SNIVDVATAK IISKEVSDGV IAPGYEPEAL NILSKKKNGK
YCILQIDPNY VPGQMESREV FGVTLQQKRN DAIINQSTFK EIVSKNKALT EQAVIDLTVA
TLVLKYTQSN SVCYAKNGMV VGLGAGQQSR IHCTRLAGDK TDNWWLRQHP KVLNMKWAKG
IKRADKSNAI DLFVTGQRIE GPEKVDYESK FEEVPEPFTK EERLEWLSKL NNVSLSSDAF
FPFPDNVYRA VQSGVKFITA PSGSVMDKVV FQAADSFDIV YVENPIRLFH H
