GenomeNet

Database: UniProt
Entry: A0A1G4IPB8_9SACH
LinkDB: A0A1G4IPB8_9SACH
Original site: A0A1G4IPB8_9SACH 
ID   A0A1G4IPB8_9SACH        Unreviewed;       482 AA.
AC   A0A1G4IPB8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   08-NOV-2023, entry version 22.
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   ORFNames=LADA_0A06040G {ECO:0000313|EMBL:SCU78522.1};
OS   Lachancea dasiensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU78522.1, ECO:0000313|Proteomes:UP000190274};
RN   [1] {ECO:0000313|EMBL:SCU78522.1, ECO:0000313|Proteomes:UP000190274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU78522.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000598,
CC         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|ARBA:ARBA00000811,
CC         ECO:0000256|RuleBase:RU361172};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}.
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       {ECO:0000256|RuleBase:RU361172}.
CC   -!- SUBUNIT: Homotetramer. Residues from neighboring subunits contribute
CC       catalytic and substrate-binding residues to each active site.
CC       {ECO:0000256|ARBA:ARBA00011668}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000256|RuleBase:RU361172}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT598460; SCU78522.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4IPB8; -.
DR   STRING; 1266660.A0A1G4IPB8; -.
DR   OrthoDB; 460764at2759; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000190274; Chromosome A.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate 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   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 {ECO:0000256|RuleBase:RU361172};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190274}.
FT   DOMAIN          374..458
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   482 AA;  53842 MW;  2E7944EF582674EE CRC64;
     MSDFDKYTTP LSSRYASEEM SSIFSLRNRF STWRKLWLNL AIAEKELGLS VITDEAIAEM
     SANLKITDED IAEASKQEAI VRHDVMAHVH AFGQTCPSAA GIIHLGATSC FVTDNADLIF
     LRDAYDVLIP KLVNVIDRLA KFAAEWKDLP VLGWTHFQPA QLTTLGKRAT LWIQELLWDL
     RNFVRARNDL GLRGVKGTTG TQASFLALFH GDHDKVEALD KRVTELLGFE TVYPVTGQTY
     SRKIDIDVLS PLSSFAATAH KMATDIRLLA NLKEIEEPFE KSQIGSSAMA YKRNPMRCER
     VCSLARHLGS LFNDAVQTAS VQWFERTLDD SAIRRISLPS AFLTADILLS TLLNISSGLV
     VYPKVIERRI MSELPFMATE NIIMAMVGKG ASRQEVHEAI RVLSHQAAAV VKEQGGDNDL
     IERIKNDQFF EPIWNELDSL LEPSTFVGRA PQQVVKFIEV DVANALAPFQ SKITDEQVKL
     SV
//
DBGET integrated database retrieval system