(data stored in SCRATCH zone)

SWISSPROT: A8LDQ8_FRASN

ID   A8LDQ8_FRASN            Unreviewed;       435 AA.
AC   A8LDQ8;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Adenylosuccinate lyase {ECO:0000256|RuleBase:RU361172};
DE            Short=ASL {ECO:0000256|RuleBase:RU361172};
DE            EC=4.3.2.2 {ECO:0000256|RuleBase:RU361172};
DE   AltName: Full=Adenylosuccinase {ECO:0000256|RuleBase:RU361172};
GN   OrderedLocusNames=Franean1_0206 {ECO:0000313|EMBL:ABW09673.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09673.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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;
CC         Xref=Rhea:RHEA:23920, ChEBI:CHEBI:29806, ChEBI:CHEBI:58443,
CC         ChEBI:CHEBI:58475; EC=4.3.2.2;
CC         Evidence={ECO:0000256|RuleBase:RU361172};
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         Evidence={ECO:0000256|RuleBase:RU361172};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC       {ECO:0000256|RuleBase:RU361172}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000256|RuleBase:RU361172}.
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DR   EMBL; CP000820; ABW09673.1; -; Genomic_DNA.
DR   RefSeq; WP_012157650.1; NC_009921.1.
DR   STRING; 298653.Franean1_0206; -.
DR   EnsemblBacteria; ABW09673; ABW09673; Franean1_0206.
DR   KEGG; fre:Franean1_0206; -.
DR   eggNOG; ENOG4107SGK; Bacteria.
DR   eggNOG; COG0015; LUCA.
DR   HOGENOM; HOG000033912; -.
DR   KO; K01756; -.
DR   OMA; HKYELWC; -.
DR   OrthoDB; 347727at2; -.
DR   BioCyc; FSP298653:G1G9X-201-MONOMER; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000001313; Chromosome.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR024083; Fumarase/histidase_N.
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   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00928; purB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8LDQ8.
DR   SWISS-2DPAGE; A8LDQ8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:ABW09673.1};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313}.
FT   DOMAIN      351    432       ADSL_C. {ECO:0000259|SMART:SM00998}.
SQ   SEQUENCE   435 AA;  46951 MW;  46098D7CF073D402 CRC64;
     MIGRYTLPDM GRVWSEANKY ELWCKVEVLV LEAHAAAGRV PADAVGPVRA AAAPTPEAVA
     EIEAVTQHDV IAFLTAWADQ TEPRSAAAYV HFGMTSSDLL DTALACQLVE ATDLLLARAD
     RLVAALRDLG LAHRGTLRVG RTHGIHGEPT VFGHRVADLA FGMARCRDRL RAARADVGVA
     KISGAVGTYS NIDTDVEGYV ADKLGLTPAP VATQVVLRDG IASWVAALAG LATVCEAVAL
     EVRHGQRTEV RELSEPFGSG QKGSSAMPHK KNPIMSERIA GIARIVRAQY VPVLEGVPLW
     HERDISHSST ERIALPDAAC GVDYLLHLTT RLVDGLVVDR ERMRANLDAT GGLVYTSAVL
     LELVETGLSR EDAYAVTQAA AMETWQTGVP FRETLRKHAG DRGLPLDEAR LDEVSRPERY
     VERLTPLFDR LAALS
//

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