O60105 (PUR8_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylosuccinate lyase
Short name=ASL
EC=4.3.2.2

Alternative name(s):
Adenylosuccinase
Short name=ASase

Gene names

Name:	ade8
ORF Names:	SPBC14F5.09c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Pathway	Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
Sequence similarities	Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 482	482	Adenylosuccinate lyase		PRO_0000137898
Sites
	Active site	83	1	Proton donor By similarity
	Active site	156	1	Proton acceptor By similarity

Sequences

	Sequence		Length	Mass (Da)
	O60105 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 945DCFD85F977E8B	FASTA	482	54,307
	10 20 30 40 50 60 MEDYGSYSTP LTARYASAEM SHLFSREMRI NTWRQLWLNL AIAEKQLGLT QITDEAIEQL 70 80 90 100 110 120 KAHVKITAPE FEIAAKEEKR QRHDVMAHIY TYGLAAPAAS GIIHLGATSC FVTDNADLIF 130 140 150 160 170 180 LRSAMDLLIP KLVNVINRLS QWSLRYKDIP TLGFTHYQPA QLTTVGKRAT LWIQELLWDL 190 200 210 220 230 240 RNFVRARNDI GFRGVKGTTG TQASFLALFE GDHAKVEELD KLVAKLSGFD NVYPVTGQTY 250 260 270 280 290 300 DRKIDIDVLQ PLASFGATAH KIATDIRLLA NLKEVEEPFE AGQIGSSAMA YKRNPMRCER 310 320 330 340 350 360 ICSQARYIMN LIPNALNTAS VQWFERTLDD SSNRRSLLPE AFLFTDSVLK ILLNVISGMV 370 380 390 400 410 420 IYPKVIQKHI RAELPFMATE NIIMAMTKHG ASRHECHEQI RVLSHQAGRV VKEEGGDNDL 430 440 450 460 470 480 IERIKNTPYF APIYDELDSL LDASTFVGRA PEQTESFVNK DVSQALAPFK SMITEEKVDL AV

References

[1]

"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: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA19327.1.
PIR	T39455.
RefSeq	NP_596735.1. NM_001022661.1.
3D structure databases
ProteinModelPortal	O60105.
SMR	O60105. Positions 6-471.
ModBase	Search...
Protein-protein interaction databases
STRING	O60105.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC14F5.09c.1; SPBC14F5.09c.1:pep; SPBC14F5.09c.
GeneID	2539985.
GenomeReviews	Gene locus ade8 in contig CU329671_GR.
KEGG	spo:SPBC14F5.09c.
NMPDR	fig|4896.1.peg.2601.
Organism-specific databases
GeneDB_Spombe	SPBC14F5.09c.
Phylogenomic databases
eggNOG	fuNOG07727.
GeneTree	EFGT00050000004719.
HOGENOM	HBG302411.
OMA	NRQDCHE.
OrthoDB	EOG4WT0JV.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004719-MONOMER.
Gene expression databases
ArrayExpress	O60105.
Family and domain databases
InterPro	IPR019468. AdenyloSucc_lyase_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR022761. Lyase1_N. IPR004769. Pur_lyase. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KO	K01756.
PANTHER	PTHR11444:SF2. PTHR11444:SF2. 1 hit.
Pfam	PF10397. ADSL_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00149. FUMRATELYASE.
SMART	SM00998. ADSL_C. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00928. PurB. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PUR8_SCHPO

Accession

Primary (citable) accession number: O60105

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program