ID PUR8_CHICK Reviewed; 485 AA.
AC P21265; A7UEA6; Q6BCQ1;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Adenylosuccinate lyase;
DE Short=ADSL;
DE Short=ASL;
DE EC=4.3.2.2 {ECO:0000250|UniProtKB:P30566};
DE AltName: Full=Adenylosuccinase;
DE Short=ASase;
GN Name=ADSL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ji C., Chen G., Zhang X.;
RT "Genomic structure, mapping and polymorphisms of adenylosuccinate lyase
RT gene in chickens.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Guan W.J., Liu C.Q., Ma Y.H.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-485.
RC TISSUE=Liver;
RX PubMed=2111814; DOI=10.1016/s0021-9258(19)38804-0;
RA Aimi J., Badylak J., Williams J., Chen Z., Zalkin H., Dixon J.E.;
RT "Cloning of a cDNA encoding adenylosuccinate lyase by functional
RT complementation in Escherichia coli.";
RL J. Biol. Chem. 265:9011-9014(1990).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11572089; DOI=10.1007/s004410100414;
RA Zhu Y., Wang M., Lin H., Li Z., Luo J.;
RT "Identification of estrogen-responsive genes in chick liver.";
RL Cell Tissue Res. 305:357-363(2001).
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|UniProtKB:P30566}.
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:0000250|UniProtKB:P30566};
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:0000250|UniProtKB:P30566};
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 {ECO:0000250|UniProtKB:P30566}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:11572089}.
CC -!- INDUCTION: Significantly increased expression by estrogen. Rapidly up-
CC regulated within 0.5 hour after extrogen exposure with a peak at 1-4
CC hours and diminishing thereafter. {ECO:0000269|PubMed:11572089}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA48574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAT76521.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY665559; AAT76521.1; ALT_INIT; Genomic_DNA.
DR EMBL; EU049886; ABU24460.1; -; mRNA.
DR EMBL; M37901; AAA48574.1; ALT_INIT; mRNA.
DR PIR; A35291; A35291.
DR RefSeq; NP_990860.1; NM_205529.1.
DR AlphaFoldDB; P21265; -.
DR SMR; P21265; -.
DR STRING; 9031.ENSGALP00000019613; -.
DR PaxDb; 9031-ENSGALP00000019613; -.
DR Ensembl; ENSGALT00010031393.1; ENSGALP00010018319.1; ENSGALG00010013095.1.
DR GeneID; 396540; -.
DR KEGG; gga:396540; -.
DR CTD; 158; -.
DR VEuPathDB; HostDB:geneid_396540; -.
DR eggNOG; KOG2700; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR InParanoid; P21265; -.
DR OMA; ASSCEKI; -.
DR OrthoDB; 460764at2759; -.
DR PhylomeDB; P21265; -.
DR Reactome; R-GGA-419140; De novo synthesis of IMP.
DR Reactome; R-GGA-421203; De novo synthesis of AMP.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR PRO; PR:P21265; -.
DR Proteomes; UP000000539; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
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; TAS:Reactome.
DR GO; GO:0097294; P:'de novo' XMP biosynthetic process; IEA:Ensembl.
DR GO; GO:0044209; P:AMP salvage; IEA:Ensembl.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:Ensembl.
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; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 2: Evidence at transcript level;
KW Lyase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..485
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000137895"
FT ACT_SITE 160
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 290
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 21..22
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250"
FT BINDING 86..88
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 112..113
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
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 335
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT CONFLICT 257
FT /note="A -> G (in Ref. 2; ABU24460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54653 MW; FCBADBF37E812CF0 CRC64;
MATPCAEEDP LARYRSPLVS RYASAEMGFN FSERKKFGTW RRLWLYLAQA EKSLGLPITD
EQIKEMEANL DNIDFKMAAE EEKKLRHDVM AHVHTFAHCC PKAAAIIHLG ATSCYVGDNT
DLIVLRDGFN LLLPKLARVI SRLADFAETH ADLPTLGFTH YQPAQLTTVG KRCCLWIQDL
CMDLQNLERA RDDLRFRGVK GTTGTQASFL QLFEGDHSKV EELDRLVTAK AGFKRSYMVT
GQTYSRKVDI EVLSVLASLG ASVHKICTDI RLLANLKEIE EPFEKDQIGS SAMPYKRNPM
RSERCCSLAR HLMTLVLDPL QTASVQWFER TLDDSANRRV CLAEAFLTAD IILSTLQNIS
EGLVVYPKVI DRRIRQELPF MATENIIMAM VKAGGNRQDC HEKIRVLSQQ AAAVVKQEGG
DNDFIARVRA DPYFSPIHEH LDSLLDPSSF TGRAPQQVAK FLKEEVRPAL IPYQSMMGGK
IELTL
//
