PUR92_YEAST
ID PUR92_YEAST Reviewed; 592 AA.
AC P38009; D6VZU3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Bifunctional purine biosynthesis protein ADE17;
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=ADE17; OrderedLocusNames=YMR120C; ORFNames=YM8564.02C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 140-150 AND 389-400.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 P38009; P54113: ADE16; NbExp=5; IntAct=EBI-14223, EBI-14213;
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 60900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
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DR EMBL; Z49273; CAA89269.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10017.1; -; Genomic_DNA.
DR PIR; S54489; S54489.
DR RefSeq; NP_013839.1; NM_001182621.1.
DR AlphaFoldDB; P38009; -.
DR SMR; P38009; -.
DR BioGRID; 35297; 117.
DR DIP; DIP-6288N; -.
DR IntAct; P38009; 38.
DR MINT; P38009; -.
DR STRING; 4932.YMR120C; -.
DR iPTMnet; P38009; -.
DR MaxQB; P38009; -.
DR PaxDb; P38009; -.
DR PRIDE; P38009; -.
DR EnsemblFungi; YMR120C_mRNA; YMR120C; YMR120C.
DR GeneID; 855149; -.
DR KEGG; sce:YMR120C; -.
DR SGD; S000004727; ADE17.
DR VEuPathDB; FungiDB:YMR120C; -.
DR eggNOG; KOG2555; Eukaryota.
DR GeneTree; ENSGT00390000004553; -.
DR HOGENOM; CLU_016316_3_2_1; -.
DR InParanoid; P38009; -.
DR OMA; WRVAKFV; -.
DR BioCyc; MetaCyc:YMR120C-MON; -.
DR BioCyc; YEAST:YMR120C-MON; -.
DR Reactome; R-SCE-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR PRO; PR:P38009; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38009; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA: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 Direct protein sequencing; Hydrolase; Multifunctional enzyme;
KW Purine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..592
FT /note="Bifunctional purine biosynthesis protein ADE17"
FT /id="PRO_0000192160"
FT DOMAIN 1..147
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT CONFLICT 389
FT /note="R -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 65263 MW; 8ABA71761B512242 CRC64;
MANYTKTAIL SVYDKTGLLD LARGLIEKNV RILASGGTAR MIRDAGFPIE DVSAITHAPE
MLGGRVKTLH PAVHGGILAR DIDSDEKDLK EQHIEKVDYV VCNLYPFKET VAKVGVTIPE
AVEEIDIGGV TLLRAAAKNH ARVTILSDPK DYSEFLSELS SNGEISQDLR NRLALKAFEH
TADYDAAISD FFRKQYSEGQ AQITLRYGAN PHQKPAQAYV SQQDSLPFKV LCGSPGYINL
LDALNSWPLV KELSASLNLP AAASFKHVSP AGAAVGIPLS DVEKQVYFVA DIENLSPLAC
AYARARGADR MSSFGDWIAL SNIVDVPTAK IISREVSDGV IAPGYEPEAL AILSKKKGGK
YCILQIDPNY VPEAVERRQV YGVTLEQKRN DAIINQSTFK EIVSQNKNLT EQAIIDLTVA
TIAIKYTQSN SVCYARNGMV VGLGAGQQSR IHCTRLAGDK ADNWWFRQHP RVLEIKWAKG
VKRPEKSNAI DLFVTGQIPT EEPELSEYQS KFEEIPKPFT PEERKEWLSK LTNVSLSSDA
FFPFPDNVYR AVKSGVKYIA APSGSVMDKV VFSAADSFDL VYVENPIRLF HH
