Reviewed, UniProtKB/Swiss-Prot Q02787 (PURA_SCHPO)

Names and origin

Protein names

Recommended name:
    Adenylosuccinate synthetase
      Short name=AMPSase
      Short name=AdSS
    EC=6.3.4.4
Alternative name(s):
    IMP--aspartate ligase

Gene names

Name:	ade2
ORF Names:	SPAC144.03

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	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Plays an important role in the de novo pathway of purine nucleotide biosynthesis.
Catalytic activity	GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the adenylosuccinate synthetase family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe response to cadmium ion Ref.1 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylosuccinate synthase activity Ref.1 Traceable author statement. Source: GeneDB_SPombe magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 434	434	Adenylosuccinate synthetase		PRO_0000095137
Regions
	Nucleotide binding	25 – 31	7	GTP Potential
Sites
	Active site	153	1	By similarity
	Active site	160	1	By similarity
	Metal binding	26	1	Magnesium By similarity
	Metal binding	53	1	Magnesium; via carbonyl oxygen By similarity
Experimental info
	Sequence conflict	100	1	E → V in AAA70333. Ref.1
	Sequence conflict	110	1	I → L in AAA70333. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q02787-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 06BF256CBD73C215	FASTA	434	47,877
	10 20 30 40 50 60 MASVRETGVN VSNDGITVVL GSQWGDEGKG KLVDILCDNV DVCARCQGGN NAGHTIVANG 70 80 90 100 110 120 VTYDFHILPS GLVNPKCQNL IGSGVVVYLP AFFSELEKLE QKGLKCRDRI FISDRAHLVF 130 140 150 160 170 180 DYHQRADALN EAELGKQSIG TTGKGIGPAY STKATRSGIR VHHLYHWAEF EARYRKNVAD 190 200 210 220 230 240 LQKRYGAFEY DVEAELIRYK ELAQRLKPFV IDAVAFMYEA LQSKKRILVE GANALMLDLD 250 260 270 280 290 300 FGTYPFVTSS NTTVGGVCTG LGVPPQRIAN SIGVVKAYTT RVGAGPFPTE QLNEIGDHLQ 310 320 330 340 350 360 SVGREVGVTT GRKRRCGWLD LVVVKYSTMI NGYTSLNLTK LDILDALDEI KVAVAYIING 370 380 390 400 410 420 KRIETFPADL DSLEEAEIVY ETFPGWKVPT TGITHWDQMP ENAKKYIEFI EKFVGVPITF 430 IGVGPGRDEM LVKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purine biosynthetic genes are required for cadmium tolerance in Schizosaccharomyces pombe." Speiser D.M., Ortiz D.F., Kreppel L., Scheel G., McDonald G., Ow D.W. Mol. Cell. Biol. 12:5301-5310(1992) [PubMed: 1448066] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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]. Strain: PR745.
[3]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M98805 mRNA. Translation: AAA70333.1. AB000538 mRNA. Translation: BAA19144.1. CU329670 Genomic DNA. Translation: CAB59683.1.
PIR	A45027. T37670.
RefSeq	NP_594664.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q02787.
Genome annotation databases
GeneID	2542823.
GenomeReviews	Gene locus ade2 in contig CU329670_GR.
KEGG	spo:SPAC144.03.
NMPDR	fig|4896.1.peg.4634.
Organism-specific databases
GeneDB_Spombe	SPAC144.03.
Phylogenomic databases
OMA	KRGRLQQ
OrthoDB	EOG9JT1P2
Enzyme and pathway databases
BRENDA	6.3.4.4. 653.
Gene expression databases
ArrayExpress	Q02787.
Family and domain databases
InterPro	IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view]
PANTHER	PTHR11846. Asucc_synthtase. 1 hit.
Pfam	PF00709. Adenylsucc_synt. 1 hit. [Graphical view]
SMART	SM00788. Adenylsucc_synt. 1 hit. [Graphical view]
TIGRFAMs	TIGR00184. purA. 1 hit.
PROSITE	PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PURA_SCHPO

Accession

Primary (citable) accession number: Q02787
Secondary accession number(s): P79061

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	December 1, 2000
Last modified:	November 24, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)