ID A0A432MNV5_9BACT Unreviewed; 476 AA.
AC A0A432MNV5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 14.
DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|RuleBase:RU361172};
DE Short=ASL {ECO:0000256|RuleBase:RU361172};
DE EC=4.3.2.2 {ECO:0000256|RuleBase:RU361172};
DE AltName: Full=Adenylosuccinase {ECO:0000256|RuleBase:RU361172};
GN ORFNames=TsocGM_03110 {ECO:0000313|EMBL:RUL89121.1};
OS Tautonia sociabilis.
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Tautonia.
OX NCBI_TaxID=2080755 {ECO:0000313|EMBL:RUL89121.1, ECO:0000313|Proteomes:UP000280296};
RN [1] {ECO:0000313|EMBL:RUL89121.1, ECO:0000313|Proteomes:UP000280296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM2012 {ECO:0000313|EMBL:RUL89121.1,
RC ECO:0000313|Proteomes:UP000280296};
RA Toschakov S.V.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RUL89121.1, ECO:0000313|Proteomes:UP000280296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM2012 {ECO:0000313|EMBL:RUL89121.1,
RC ECO:0000313|Proteomes:UP000280296};
RA Kovaleva O.L., Elcheninov A.G., Van Heerden E., Toshchakov S.V.,
RA Novikov A., Bonch-Osmolovskaya E.A., Kublanov I.V.;
RT "Tautonia sociabilis, a novel thermotolerant planctomycete of
RT Isosphaeraceae family, isolated from a 4000 m deep subterranean habitat.";
RL Submitted (JAN-2019) 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|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|RuleBase:RU361172}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {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:RUL89121.1}.
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DR EMBL; RYZH01000004; RUL89121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432MNV5; -.
DR OrthoDB; 9768878at2; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000280296; 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; 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; 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:RUL89121.1};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000280296}.
FT DOMAIN 371..453
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 476 AA; 53173 MW; 41AAD01A6C3D6C10 CRC64;
MMNHDTYENP LISRYASRAM AELWSSNRKF STWRRLWVAL ARAEKELGLE ISDAQIAAME
AKVDAIDFEA ARAYEKKLRH DVMAHVHTFG DAAPEARAII HLGATSCYVT DNTDLILLRE
ALGRVRDQLV GAIDALAVFA ERWKGEPCLG YTHFQPAQLV TIGKRATLWC QDLLLDLDEI
ERRIAELRFL GVKGTTGTQA SFLDLFDGDH AKVEELDRRV AAAFGFDRVF PVTGQTYPRK
VDSLVLSALV GLAESAHRFG SDLRLLAHER ELEEPFEADQ IGSSAMAYKR NPMRAERLCS
IARFLMAQHA AASQTAATQW LERTLDDSAV RRMTLPQSFL AADALLTLYL NVVPGLVVRP
AVVAAHVERE LPFMATEAIL MAGVRAGGDR QDLHERIRVH SLAAADAVKQ GADRNDLIDR
LQADPAFAAV DLDATLDPRR FIGRCPQQVD AFLDTEVEPV RRRYPNLRGQ RQEVHV
//
