ID PUR8_SCHPO Reviewed; 482 AA.
AC O60105;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 24-JAN-2024, entry version 154.
DE RecName: Full=Adenylosuccinate lyase;
DE Short=ASL;
DE EC=4.3.2.2;
DE AltName: Full=Adenylosuccinase;
DE Short=ASase;
GN Name=ade8; ORFNames=SPBC14F5.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate;
CC Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567,
CC ChEBI:CHEBI:456215; EC=4.3.2.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920,
CC ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2;
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 2/2.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC catalytic and substrate-binding residues to each active site (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA19327.1; -; Genomic_DNA.
DR PIR; T39455; T39455.
DR RefSeq; NP_596735.1; NM_001022661.2.
DR AlphaFoldDB; O60105; -.
DR SMR; O60105; -.
DR BioGRID; 276529; 6.
DR STRING; 284812.O60105; -.
DR iPTMnet; O60105; -.
DR MaxQB; O60105; -.
DR PaxDb; 4896-SPBC14F5-09c-1; -.
DR EnsemblFungi; SPBC14F5.09c.1; SPBC14F5.09c.1:pep; SPBC14F5.09c.
DR GeneID; 2539985; -.
DR KEGG; spo:SPBC14F5.09c; -.
DR PomBase; SPBC14F5.09c; ade8.
DR VEuPathDB; FungiDB:SPBC14F5.09c; -.
DR eggNOG; KOG2700; Eukaryota.
DR HOGENOM; CLU_030949_1_1_1; -.
DR InParanoid; O60105; -.
DR OMA; ASSCEKI; -.
DR PhylomeDB; O60105; -.
DR Reactome; R-SPO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR PRO; PR:O60105; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IDA:PomBase.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IDA:PomBase.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IDA:PomBase.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; ISO:PomBase.
DR GO; GO:0006106; P:fumarate metabolic process; IDA:PomBase.
DR CDD; cd03302; Adenylsuccinate_lyase_2; 1.
DR Gene3D; 1.10.275.60; -; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR InterPro; IPR019468; AdenyloSucc_lyase_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR004769; Pur_lyase.
DR NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..482
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000137898"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 286
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 14..15
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250"
FT BINDING 82..84
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 108..109
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 482 AA; 54307 MW; 945DCFD85F977E8B CRC64;
MEDYGSYSTP LTARYASAEM SHLFSREMRI NTWRQLWLNL AIAEKQLGLT QITDEAIEQL
KAHVKITAPE FEIAAKEEKR QRHDVMAHIY TYGLAAPAAS GIIHLGATSC FVTDNADLIF
LRSAMDLLIP KLVNVINRLS QWSLRYKDIP TLGFTHYQPA QLTTVGKRAT LWIQELLWDL
RNFVRARNDI GFRGVKGTTG TQASFLALFE GDHAKVEELD KLVAKLSGFD NVYPVTGQTY
DRKIDIDVLQ PLASFGATAH KIATDIRLLA NLKEVEEPFE AGQIGSSAMA YKRNPMRCER
ICSQARYIMN LIPNALNTAS VQWFERTLDD SSNRRSLLPE AFLFTDSVLK ILLNVISGMV
IYPKVIQKHI RAELPFMATE NIIMAMTKHG ASRHECHEQI RVLSHQAGRV VKEEGGDNDL
IERIKNTPYF APIYDELDSL LDASTFVGRA PEQTESFVNK DVSQALAPFK SMITEEKVDL
AV
//
