Reviewed, UniProtKB/Swiss-Prot P54113 (PUR91_YEAST)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthesis protein ADE16
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC

Gene names

Name:	ADE16
Ordered Locus Names:	YLR028C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.
Subunit structure	Homodimer (Possible).
Domain	The IMP cyclohydrolase activity resides in the N-terminal region By similarity.
Miscellaneous	Present with 7700 molecules/cell in log phase SD medium. Ref.3
Sequence similarities	Belongs to the purH family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from direct assay. Source: SGD aerobic respiration Inferred from expression pattern. Source: SGD ascospore formation Inferred from expression pattern. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD
Molecular function	IMP cyclohydrolase activity Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-14213,EBI-14213
AAT2	P23542	1	EBI-14213,EBI-2002
ADE17	P38009	1	EBI-14213,EBI-14223
ARO8	P53090	1	EBI-14213,EBI-2042933
CAR2	P07991	1	EBI-14213,EBI-12430
CYS4	P32582	1	EBI-14213,EBI-4167
GLN1	P32288	1	EBI-14213,EBI-7665
HEX2	Q00816	1	EBI-14213,EBI-8270
HSP12	P22943	1	EBI-14213,EBI-8548
HUG1	Q6Q5K6	1	EBI-14213,EBI-392766
IPP1	P00817	1	EBI-14213,EBI-9338
LSP1	Q12230	1	EBI-14213,EBI-34978
RAD25	Q00578	1	EBI-14213,EBI-14683
RNR1	P21524	1	EBI-14213,EBI-15234
VAS1	P07806-1	1	EBI-14213,EBI-1009942
VMA4	P22203	1	EBI-14213,EBI-20268
VMA8	P32610	1	EBI-14213,EBI-20264

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 591	591	Bifunctional purine biosynthesis protein ADE16		PRO_0000192159

Sequences

	Sequence		Length	Mass (Da)
	P54113-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DEC06684BFED7CA7	FASTA	591	65,282
	10 20 30 40 50 60 MGKYTKTAIL SVYDKTGLLD LAKGLVENNV RILASGGTAN MVREAGFPVD DVSSITHAPE 70 80 90 100 110 120 MLGGRVKTLH PAVHAGILAR NLEGDEKDLK EQHIDKVDFV VCNLYPFKET VAKIGVTVQE 130 140 150 160 170 180 AVEEIDIGGV TLLRAAAKNH SRVTILSDPN DYSIFLQDLS KDGEISQDLR NRFALKAFEH 190 200 210 220 230 240 TADYDAAISD FFRKQYSEGK AQLPLRYGCN PHQRPAQAYI TQQEELPFKV LCGTPGYINL 250 260 270 280 290 300 LDALNSWPLV KELSASLNLP AAASFKHVSP AGAAVGLPLS DVERQVYFVN DMEDLSPLAC 310 320 330 340 350 360 AYARARGADR MSSFGDFIAL SNIVDVATAK IISKEVSDGV IAPGYEPEAL NILSKKKNGK 370 380 390 400 410 420 YCILQIDPNY VPGQMESREV FGVTLQQKRN DAIINQSTFK EIVSKNKALT EQAVIDLTVA 430 440 450 460 470 480 TLVLKYTQSN SVCYAKNGMV VGLGAGQQSR IHCTRLAGDK TDNWWLRQHP KVLNMKWAKG 490 500 510 520 530 540 IKRADKSNAI DLFVTGQRIE GPEKVDYESK FEEVPEPFTK EERLEWLSKL NNVSLSSDAF 550 560 570 580 590 FPFPDNVYRA VQSGVKFITA PSGSVMDKVV FQAADSFDIV YVENPIRLFH H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Tibbetts A.S., Appling D.R. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U62402 Genomic DNA. Translation: AAB57774.1. Z73200 Genomic DNA. Translation: CAA97552.1.
PIR	S77707.
RefSeq	NP_013128.1.
3D structure databases
HSSP	HSSP built from PDB template 1G8M based on UniProtKB P31335.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4657N.
IntAct	P54113. 32 interactions.
STRING	P54113.
Proteomic databases
PeptideAtlas	P54113.
Genome annotation databases
Ensembl	YLR028C; YLR028C; YLR028C; Saccharomyces cerevisiae. [Genome view]
GeneID	850715.
GenomeReviews	Gene locus YLR028C in contig Y13138_GR.
KEGG	sce:YLR028C.
NMPDR	fig|4932.3.peg.4119.
Organism-specific databases
CYGD	YLR028c.
SGD	S000004018. ADE16.
Phylogenomic databases
HOGENOM	P54113.
OMA	MSSYGDF.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-501.
BRENDA	2.1.2.3. 250. 3.5.4.10. 250.
Gene expression databases
ArrayExpress	P54113.
Genevestigator	P54113.
GermOnline	YLR028C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002695. AICARFT_IMPCHas. IPR013982. AICARFT_IMPCHas_formly. IPR011607. MGS. [Graphical view]
PANTHER	PTHR11692. AICARFT_IMPCHas. 1 hit.
Pfam	PF01808. AICARFT_IMPCHas. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PIRSF	PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMART	SM00798. AICARFT_IMPCHas. 1 hit. [Graphical view]
TIGRFAMs	TIGR00355. purH. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	966781.

Entry information

Entry name

PUR91_YEAST

Accession

Primary (citable) accession number: P54113

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)