PUR8_CAEEL
ID PUR8_CAEEL Reviewed; 478 AA.
AC Q21774; Q8I4G8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Adenylosuccinate lyase;
DE Short=ASL;
DE EC=4.3.2.2;
DE AltName: Full=Adenylosuccinase;
DE Short=ASase;
GN Name=adsl-1 {ECO:0000312|WormBase:R06C7.5a};
GN ORFNames=R06C7.5 {ECO:0000312|WormBase:R06C7.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND SUBUNIT.
RG Southeast collaboratory for structural genomics (SECSG);
RT "Structural genomics of Caenorhabditis elegans: adenylosuccinate lyase.";
RL Submitted (FEB-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes two non-sequential steps in de novo AMP synthesis:
CC converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole-4-carboxamide, and thereby also contributes to de
CC novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP)
CC to AMP and fumarate. {ECO:0000250}.
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
CC (Probable). {ECO:0000305|Ref.2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:R06C7.5a};
CC IsoId=Q21774-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:R06C7.5b};
CC IsoId=Q21774-2; Sequence=VSP_016396, VSP_016397;
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; Z71266; CAA95843.1; -; Genomic_DNA.
DR EMBL; Z71266; CAD56593.1; -; Genomic_DNA.
DR PIR; T23969; T23969.
DR RefSeq; NP_492049.1; NM_059648.5. [Q21774-1]
DR RefSeq; NP_871850.1; NM_182050.3.
DR PDB; 1YIS; X-ray; 2.40 A; A=1-478.
DR PDBsum; 1YIS; -.
DR AlphaFoldDB; Q21774; -.
DR SMR; Q21774; -.
DR BioGRID; 37909; 18.
DR STRING; 6239.R06C7.5a; -.
DR EPD; Q21774; -.
DR PaxDb; Q21774; -.
DR PeptideAtlas; Q21774; -.
DR EnsemblMetazoa; R06C7.5a.1; R06C7.5a.1; WBGene00011064. [Q21774-1]
DR EnsemblMetazoa; R06C7.5b.1; R06C7.5b.1; WBGene00011064. [Q21774-2]
DR GeneID; 172466; -.
DR KEGG; cel:CELE_R06C7.5; -.
DR UCSC; R06C7.5a; c. elegans. [Q21774-1]
DR CTD; 172466; -.
DR WormBase; R06C7.5a; CE06248; WBGene00011064; adsl-1. [Q21774-1]
DR WormBase; R06C7.5b; CE32476; WBGene00011064; adsl-1. [Q21774-2]
DR eggNOG; KOG2700; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_030949_1_1_1; -.
DR InParanoid; Q21774; -.
DR OMA; ASSCEKI; -.
DR OrthoDB; 904932at2759; -.
DR PhylomeDB; Q21774; -.
DR Reactome; R-CEL-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR EvolutionaryTrace; Q21774; -.
DR PRO; PR:Q21774; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011064; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IBA:GO_Central.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IBA:GO_Central.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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 Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lyase; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..478
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000137897"
FT ACT_SITE 155
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 285
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 81..83
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 107..108
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 353..370
FT /note="NIFEGLSVQTDNVKKIVE -> VSVLKITSSKDLVYKQTM (in isoform
FT b)"
FT /evidence="ECO:0000305"
FT /id="VSP_016396"
FT VAR_SEQ 371..478
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_016397"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 27..47
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 108..144
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1YIS"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:1YIS"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 164..188
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:1YIS"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 242..270
FT /evidence="ECO:0007829|PDB:1YIS"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 330..357
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 362..384
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:1YIS"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 440..443
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 459..463
FT /evidence="ECO:0007829|PDB:1YIS"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:1YIS"
SQ SEQUENCE 478 AA; 53569 MW; 0E7FAA122D32774F CRC64;
MASEDKFESV LSTRYCKNSP LVSILSETNK ATLWRQLWIW LAEAEKELGL KQVTQDAIDE
MKSNRDVFDW PFIRSEERKL KHDVMAHNHA FGKLCPTAAG IIHLGATSCF VQDNADLIAY
RDSIDHILKR FATVIDRLAA FSLKNKEVVT VGRTHYQTAS LVTVGKRGVL WAQELLMAFQ
SLSEFRDKMR FRGIKGATGT QDSFLTLFAG DESKVEALDE LVTKKANFSN RFLITGQTYS
RQQDSQLVFS LSLLGAAAKK VCTDIRVLQA FGELLEPFEK DQIGSSAMPY KKNPMKSERC
CALSRKLINA PQEALTILAD QGLERTLDDS AGRRMLIPDV LLTAEALLTT LQNIFEGLSV
QTDNVKKIVE DEIAFLGLEK AMMMLTEEGV DRQQAHAVIR KTALEAKQLQ ATQKVDIRQT
MADPFFDSVR DRVVGLVNNP INFTGRCVSQ TESFIAKELK PTIDKYLDKS AGNVQLDV
