PUR8_MACFA
ID PUR8_MACFA Reviewed; 484 AA.
AC Q8HXY5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
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; ORFNames=QflA-14811;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; AB083304; BAC20583.1; -; mRNA.
DR AlphaFoldDB; Q8HXY5; -.
DR SMR; Q8HXY5; -.
DR STRING; 9541.XP_005567256.1; -.
DR VEuPathDB; HostDB:ENSMFAG00000039307; -.
DR eggNOG; KOG2700; Eukaryota.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000233100; Chromosome 10.
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 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 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 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Lyase; Purine biosynthesis;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30566"
FT CHAIN 2..484
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000137893"
FT ACT_SITE 159
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 289
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 20..21
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250"
FT BINDING 85..87
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 111..112
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250"
FT BINDING 329
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 BINDING 338
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P30566"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30566"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30566"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P30566"
SQ SEQUENCE 484 AA; 54894 MW; 94B88B660692342A CRC64;
MAAVGDHGSP DSYRSPLASR YASPEMCFVF SDRYKFRTWR QLWLWLAEAE QTLGLPITDE
QIQEMKSNLD NIDFKMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD
LIILRNALDL LLPKLARVIS RLADFAKERA SLPTLGFTHF QPAQLTTVGK RCCLWIQDLC
MDLQNLKRVR DDLRFRGVKG TTGTQASFLQ LFEGDDHKVE QLDKMVTDKA GFKRAFIITG
QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR
SERCCSLARH LMTLVMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE
GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH EKIRVLSQQA ASVVKQEGGD
NDLIERIQAD AYFSPIHSQL DRLLDPSSFT GRASQQVQRF LEEEVYPLLK PYESVMKVKA
ELCL
