ID   PUR8_YEAST              Reviewed;         482 AA.
AC   Q05911;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 85.
DE   RecName: Full=Adenylosuccinate lyase;
DE            Short=ASL;
DE            EC=4.3.2.2;
DE   AltName: Full=Adenylosuccinase;
DE            Short=ASase;
GN   Name=ADE13; OrderedLocusNames=YLR359W; ORFNames=L8039.12;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196, AND MASS
RP   SPECTROMETRY.
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
RA   Marsischky G., Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4 AND THR-9, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
CC   -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-
CC       (5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 2/2.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 5/5.
CC   -!- INTERACTION:
CC       P38148:PPS1; NbExp=1; IntAct=EBI-14263, EBI-21161;
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily.
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DR   EMBL; U19103; AAB67573.1; -; Genomic_DNA.
DR   EMBL; U19102; AAB67755.2; -; Genomic_DNA.
DR   PIR; S51377; S51377.
DR   RefSeq; NP_013463.1; -.
DR   DIP; DIP:2787N; -.
DR   IntAct; Q05911; 7.
DR   PeptideAtlas; Q05911; -.
DR   Ensembl; YLR359W; Saccharomyces cerevisiae.
DR   GeneID; 851073; -.
DR   GenomeReviews; Y13138_GR; YLR359W.
DR   KEGG; sce:YLR359W; -.
DR   NMPDR; fig|4932.3.peg.4485; -.
DR   CYGD; YLR359w; -.
DR   SGD; S000004351; ADE13.
DR   HOGENOM; Q05911; -.
DR   OMA; Q05911; NRQDCHE.
DR   BioCyc; MetaCyc:MON-489; -.
DR   BRENDA; 4.3.2.2; 250.
DR   NextBio; 967720; -.
DR   GermOnline; YLR359W; Saccharomyces cerevisiae.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imida...; IEA:EC.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumar...; IMP:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:SGD.
DR   InterPro; IPR019468; Adenylosuccinate_lyase_C.
DR   InterPro; IPR000362; Fumarate_lyase.
DR   InterPro; IPR004769; Pur_lyase.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   TIGRFAMs; TIGR00928; purB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Isopeptide bond; Lyase; Phosphoprotein;
KW   Purine biosynthesis; Ubl conjugation.
FT   CHAIN         1    482       Adenylosuccinate lyase.
FT                                /FTId=PRO_0000137899.
FT   ACT_SITE     83     83       Proton donor (By similarity).
FT   ACT_SITE    156    156       Proton acceptor (By similarity).
FT   MOD_RES       4      4       Phosphotyrosine.
FT   MOD_RES       9      9       Phosphothreonine.
FT   CROSSLNK    196    196       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
SQ   SEQUENCE   482 AA;  54510 MW;  AED9468B7828AB77 CRC64;
     MPDYDNYTTP LSSRYASKEM SATFSLRNRF STWRKLWLNL AIAEKELGLT VVTDEAIEQM
     RKHVEITDDE IAKASAQEAI VRHDVMAHVH TFGETCPAAA GIIHLGATSC FVTDNADLIF
     IRDAYDIIIP KLVNVINRLA KFAMEYKDLP VLGWTHFQPA QLTTLGKRAT LWIQELLWDL
     RNFERARNDI GLRGVKGTTG TQASFLALFH GNHDKVEALD ERVTELLGFD KVYPVTGQTY
     SRKIDIDVLA PLSSFAATAH KMATDIRLLA NLKEVEEPFE KSQIGSSAMA YKRNPMRCER
     VCSLARHLGS LFSDAVQTAS VQWFERTLDD SAIRRISLPS AFLTADILLS TLLNISSGLV
     VYPKVIERRI KGELPFMATE NIIMAMVEKN ASRQEVHERI RVLSHQAAAV VKEEGGENDL
     IERVKRDEFF KPIWEELDSL LEPSTFVGRA PQQVEKFVQK DVNNALQPFQ KYLNDEQVKL
     NV
//