Reviewed, UniProtKB/Swiss-Prot O74928 (PUR9_SCHPO)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthesis protein ade10
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:	ade10
ORF Names:	SPCPB16A4.03c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	585 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity.
Domain	The IMP cyclohydrolase activity resides in the N-terminal region By similarity.
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	IMP biosynthetic process Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	IMP cyclohydrolase activity Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe phosphoribosylaminoimidazolecarboxamide formyltransferase activity Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 585	585	Bifunctional purine biosynthesis protein ade10		PRO_0000192158
Experimental info
	Sequence conflict	404	1	K → Q in BAA13904. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O74928-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 103031D3F957529F	FASTA	585	64,123
	10 20 30 40 50 60 MYALLSVYDK TGLLELAKAL TSKGVKLLGS GGTAKMIRES GMEVADVSSI TNAPEILGGR 70 80 90 100 110 120 VKTLHPAVHG GILARDIPSD EKDLVEQSIE KIDIVVCNLY PFRETIAKPN VTIPEAVEEI 130 140 150 160 170 180 DIGGVTLLRA AAKNHARVTI LSDPADYATF TDKFLSDKLT QDDRNTYALK AFASTASYDA 190 200 210 220 230 240 AITDYFRKQY AAGVDQLTLR YGANPHQSPA QAFMEQGPLP FKVLCGSPGY INLMDALNSW 250 260 270 280 290 300 PLVKELRENI GIPAAASFKH VSPAGAAVGL PLSDVEKKVY FVSDITEFTP LACAYARARG 310 320 330 340 350 360 ADRMSSFGDF IALSDTVDVC TARIISREVS DGVIAPGYEP EALELLKKKK GGKYCVLQMD 370 380 390 400 410 420 PKYVPAEIET RQVYGISLQQ HRNHAKIDFS LFEKVVSKNK DLPKSALIDL VIATTALKYT 430 440 450 460 470 480 QSNSVCYAKN GMVVGLGAGQ QSRIHCNRLA GDKADNWWLR HHPKVLGMQF KKSAKRPEKS 490 500 510 520 530 540 NAIDLYVLDA VPAEGSEREQ WESAFETIPE PLTKKEREEF LATCKDVVCA SDAFFPFPDN 550 560 570 580 IYRLAQSGVK YVAAPGGSVM DQAVRDTANE FNMVFSEIPL RLFHH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of the Schizosaccharomyces pombe ade10+ gene." Liedtke C., Schmidt H. Yeast 14:1307-1310(1998) [PubMed: 9802209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-585. Strain: PR745.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y16419 Genomic DNA. Translation: CAA76207.1. CU329672 Genomic DNA. Translation: CAC39322.1. D89243 mRNA. Translation: BAA13904.1.
PIR	T43150.
RefSeq	NP_588027.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O74928.
Genome annotation databases
GeneID	2539569.
GenomeReviews	Gene locus ade10 in contig CU329672_GR.
KEGG	spo:SPCPB16A4.03c.
NMPDR	fig|4896.1.peg.365.
Organism-specific databases
GeneDB_Spombe	SPCPB16A4.03c.
Phylogenomic databases
HOGENOM	HBG498048.
OMA	VVKHVKS.
OrthoDB	EOG94BCJN.
Enzyme and pathway databases
BRENDA	2.1.2.3. 653. 3.5.4.10. 653.
Gene expression databases
ArrayExpress	O74928.
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. SM00851. MGS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR9_SCHPO

Accession

Primary (citable) accession number: O74928
Secondary accession number(s): P78892

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	November 1, 1998
Last modified:	December 15, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)