ID A0A0D9QQM5_PLAFR Unreviewed; 464 AA.
AC A0A0D9QQM5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058, ECO:0000256|RuleBase:RU361172};
DE Short=ASL {ECO:0000256|RuleBase:RU361172};
DE EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339, ECO:0000256|RuleBase:RU361172};
DE AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717, ECO:0000256|RuleBase:RU361172};
GN ORFNames=AK88_01365 {ECO:0000313|EMBL:KJP89072.1};
OS Plasmodium fragile.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5857 {ECO:0000313|EMBL:KJP89072.1, ECO:0000313|Proteomes:UP000054561};
RN [1] {ECO:0000313|EMBL:KJP89072.1, ECO:0000313|Proteomes:UP000054561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=nilgiri {ECO:0000313|Proteomes:UP000054561};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Duraisingh M., Young S.K., Zeng Q., Gargeya S., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium fragile nilgiri.";
RL Submitted (MAR-2014) 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|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; AMP
CC from IMP: step 2/2. {ECO:0000256|ARBA:ARBA00004734,
CC 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|ARBA:ARBA00004706, ECO:0000256|RuleBase:RU361172}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00008273,
CC ECO:0000256|RuleBase:RU361172}.
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DR EMBL; KQ001655; KJP89072.1; -; Genomic_DNA.
DR RefSeq; XP_012334423.1; XM_012479000.1.
DR AlphaFoldDB; A0A0D9QQM5; -.
DR EnsemblProtists; KJP89072; KJP89072; AK88_01365.
DR GeneID; 24266679; -.
DR VEuPathDB; PlasmoDB:AK88_01365; -.
DR OMA; NNWAVVA; -.
DR OrthoDB; 203956at2759; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000054561; Unassembled WGS sequence.
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; cd01598; PurB; 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 Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
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 InterPro; IPR047136; PurB_bact.
DR InterPro; IPR013539; PurB_C.
DR NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF08328; ASL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361172};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|RuleBase:RU361172}.
FT DOMAIN 12..311
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 330..446
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 464 AA; 53469 MW; EAFD39B1FB36EB72 CRC64;
MDHLKNISPI DGRYKKSCSE ISAFFSEYAL IKHRIIVEVR WLLFLNEKEL FFKKVSAQSV
EELNQIETNI TDSDIARVKE IEEETNHDVK AVEYFVKEKL SKSGREDLVK IKEYVHYLCT
SEDINNVAYA MCLKVCLQDI IIPCMEKIML KLKELAVEYS DVPLLSRTHG QPASSTTFGK
EMANFYSRIH HHVEVIRGVK IYAKFNGAVG NFNAHKVVSK NTDWIGHIKI FLQKYFDLTY
GLYCTQIQDH DYICEVCDGL ARANATLIDL CVDIWLYISN NLLKLKLKDK EVGSSTMPHK
VNPIDFENAE GNLHVANAFL KLFSSKLPTS RLQRDLSDST VLRNIGSSLA YCLIAYKSVL
KGLNKMDLDR RKLEEELNEN WSTLAEPIQI MMKRFNYVDA YEELKQFTRG KIVDKEIMQE
FIKTKCNFLP QDVVDQLLQL TPATYTGYAD YLAKNVERLS GQLD
//
