ID A0A0D6P4K1_9PROT Unreviewed; 458 AA.
AC A0A0D6P4K1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 08-NOV-2023, entry version 26.
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=Asru_0053_08 {ECO:0000313|EMBL:GAN76113.1};
OS Acidisphaera rubrifaciens HS-AP3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidisphaera.
OX NCBI_TaxID=1231350 {ECO:0000313|EMBL:GAN76113.1, ECO:0000313|Proteomes:UP000032680};
RN [1] {ECO:0000313|EMBL:GAN76113.1, ECO:0000313|Proteomes:UP000032680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-AP3 {ECO:0000313|EMBL:GAN76113.1,
RC ECO:0000313|Proteomes:UP000032680};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidisphaera rubrifaciens HS-AP3.";
RL Submitted (NOV-2012) 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:ARBA00024477};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921;
CC Evidence={ECO:0000256|ARBA:ARBA00024477};
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:ARBA00024487};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854;
CC Evidence={ECO:0000256|ARBA:ARBA00024487};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAN76113.1}.
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DR EMBL; BANB01000053; GAN76113.1; -; Genomic_DNA.
DR RefSeq; WP_048859891.1; NZ_BANB01000053.1.
DR AlphaFoldDB; A0A0D6P4K1; -.
DR OrthoDB; 9768878at2; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000032680; 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; cd01360; Adenylsuccinate_lyase_1; 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; IPR019468; AdenyloSucc_lyase_C.
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 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 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:GAN76113.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000032680}.
FT DOMAIN 357..442
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 458 AA; 49356 MW; A46AAFD9318E1EED CRC64;
MVPRYTRPEM AAIWAPENRY GIWFEIEALA AEAMAEAGDI PAEAARAIRA RGAPALAAIG
PADIERIDAI ERETRHDVIA FLTWLAEAIG PDSRFVHQGL TSSDVLDTCL SVQMTQAADL
LLADLDAVLA ALKRRAFEHR DTLTIGRSHG IHAEPTTFGL KLAGHYAEFA RNRARLLAAR
AEVAVCAISG AVGTYAHVDP RVETYVAERL GLVPETHSTQ VIPRDRHAAF FCTLGLIASA
IERLATEVRH LQRSEVREAE EFFHPGQKGS SAMPHKRNPV LSENLTGLAR VVRAAVTPAL
ENVALWHERD ISHSSVERVI APDATMALDF ALARLAGMME KLTIYPDRMA ANLDSLGGVV
HSGEVLLALT RAGILREDAY RIVQRNAMAT WEGLGQPGAR SFRDNLLADA EVAGRVDAAT
IDAALDPAFH RRQVGAIFAR VFGAEDPAAG GAAHGGAG
//
