P54113 (PUR91_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional purine biosynthesis protein ADE16

Including the following 2 domains:

1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
   EC=2.1.2.3
   Alternative name(s):
   5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
   AICAR transformylase
2. IMP cyclohydrolase
   EC=3.5.4.10
   Alternative name(s):
   ATIC
   IMP synthase
   Inosinicase

Gene names

Name:	ADE16
Ordered Locus Names:	YLR028C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	591 AA.
Sequence status	Complete.
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.
Sequence similarities	Belongs to the PurH family.
Sequence caution	The sequence CAA97551.2 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from direct assay PubMed 10877846. Source: SGD aerobic respiration Inferred from expression pattern PubMed 10877846. Source: SGD ascospore formation Inferred from expression pattern PubMed 10877846. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 10877846. Source: SGD
Molecular_function	IMP cyclohydrolase activity Inferred from direct assay PubMed 10877846. Source: SGD phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from direct assay PubMed 10877846. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADE17	P38009	3	EBI-14213,EBI-14223

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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62402 Genomic DNA. Translation: AAB57774.1. Z73199 Genomic DNA. Translation: CAA97551.2. Sequence problems. Z73200 Genomic DNA. Translation: CAA97552.1. BK006945 Genomic DNA. Translation: DAA09346.1.
PIR	S77707.
RefSeq	NP_013128.1. NM_001181915.1.
3D structure databases
ProteinModelPortal	P54113.
SMR	P54113. Positions 6-591.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4657N.
IntAct	P54113. 16 interactions.
MINT	MINT-477775.
STRING	4932.YLR028C.
Proteomic databases
PaxDb	P54113.
PeptideAtlas	P54113.
PRIDE	P54113.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR028C; YLR028C; YLR028C.
GeneID	850715.
KEGG	sce:YLR028C.
Organism-specific databases
CYGD	YLR028c.
SGD	S000004018. ADE16.
Phylogenomic databases
eggNOG	COG0138.
GeneTree	ENSGT00390000004553.
HOGENOM	HOG000230372.
KO	K00602.
OMA	DRDNTID.
OrthoDB	EOG4D82DW.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-501.
UniPathway	UPA00074; UER00133. UPA00074; UER00135.
Gene expression databases
Genevestigator	P54113.
GermOnline	YLR028C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.287.440. 1 hit. 3.40.140.20. 3 hits. 3.40.50.1380. 1 hit.
InterPro	IPR024051. AICAR_Tfase_dom. IPR024050. AICAR_Tfase_insert_dom. IPR002695. AICARFT_IMPCHas. IPR016193. Cytidine_deaminase-like. IPR011607. MGS-like_dom. [Graphical view]
PANTHER	PTHR11692. PTHR11692. 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. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit. SSF52335. MGS-like_dom. 1 hit.
TIGRFAMs	TIGR00355. purH. 1 hit.
ProtoNet	Search...
Other
NextBio	966781.

Entry information

Entry name

PUR91_YEAST

Accession

Primary (citable) accession number: P54113
Secondary accession number(s): D6VY30, E9PAG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program