ID F2L1K3_THEU7 Unreviewed; 407 AA.
AC F2L1K3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058};
DE EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339};
DE AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717};
GN OrderedLocusNames=TUZN_0173 {ECO:0000313|EMBL:AEA11673.1};
OS Thermoproteus uzoniensis (strain 768-20).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=999630 {ECO:0000313|EMBL:AEA11673.1, ECO:0000313|Proteomes:UP000008138};
RN [1] {ECO:0000313|EMBL:AEA11673.1, ECO:0000313|Proteomes:UP000008138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-20 {ECO:0000313|EMBL:AEA11673.1,
RC ECO:0000313|Proteomes:UP000008138};
RX PubMed=21478349; DOI=10.1128/JB.00409-11;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL J. Bacteriol. 193:3156-3157(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=768-20;
RA Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of the thermoacidophilic crenarchaeon
RT Thermoproteus uzoniensis 768-20.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC and fumarate. {ECO:0000256|ARBA:ARBA00025012}.
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00008273}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002590; AEA11673.1; -; Genomic_DNA.
DR RefSeq; WP_013679009.1; NC_015315.1.
DR AlphaFoldDB; F2L1K3; -.
DR STRING; 999630.TUZN_0173; -.
DR GeneID; 10359722; -.
DR KEGG; tuz:TUZN_0173; -.
DR eggNOG; arCOG01747; Archaea.
DR HOGENOM; CLU_030949_0_1_2; -.
DR OrthoDB; 26319at2157; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000008138; Chromosome.
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 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; 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; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AEA11673.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 83..286
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
SQ SEQUENCE 407 AA; 45383 MW; 600CFEF11807FD20 CRC64;
MEPISPFDWR YGSEELRRLF SRQSIVDAYL EVERALVCAL EELGVAERGC CEAASRASIS
AEEVYRLERE LRHDVLALVQ LLEERSGCRF VHYGATSNDV IDTAWALLIR RALGAIKERG
RAVAEELRRL ALKYADLPAV GRTHGQWAEP ITLGFKFANY YYELYIACRA LYAAEEHVRG
KLGGAVGTMA SWGPLGLKLR EAVSRRLGVP FHPISTQVAP RESFAFLASA LALLAGFAER
LATEVRELSR PEIGEVFETV GGGSSAMPHK ANPTNSERVV SLARYVRSLL VVAHENIALW
HERDLTNSAN ERVWIPEALL AVDEILATTA RVLRTLHVDE ERVRRNLEAA LPQITSEFRM
LELVRKGMRR AEAYRAARAE GGSGELPRGW PVRELIDSAL ALEACPQ
//
