ID G0EDW7_PYRF1 Unreviewed; 452 AA.
AC G0EDW7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 OrderedLocusNames=Pyrfu_0867 {ECO:0000313|EMBL:AEM38736.1};
OS Pyrolobus fumarii (strain DSM 11204 / 1A).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrolobus.
OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM38736.1, ECO:0000313|Proteomes:UP000001037};
RN [1] {ECO:0000313|EMBL:AEM38736.1, ECO:0000313|Proteomes:UP000001037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX PubMed=21886865;
RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H.,
RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT Pyrolobus fumarii type strain (1A).";
RL Stand. Genomic Sci. 4:381-392(2011).
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|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}.
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DR EMBL; CP002838; AEM38736.1; -; Genomic_DNA.
DR RefSeq; WP_014026413.1; NC_015931.1.
DR AlphaFoldDB; G0EDW7; -.
DR STRING; 694429.Pyrfu_0867; -.
DR GeneID; 11139341; -.
DR KEGG; pfm:Pyrfu_0867; -.
DR eggNOG; arCOG01747; Archaea.
DR HOGENOM; CLU_030949_0_1_2; -.
DR InParanoid; G0EDW7; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000001037; 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 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 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:AEM38736.1};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000001037}.
FT DOMAIN 362..442
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 452 AA; 50345 MW; 27A2D80C65961DEA CRC64;
MCVFEWRYGS KEMRDLLSLE SWMRHLLRVE VAVVEAMEEL GLAPGGIAAK VRDAAESITV
KEWLEAEKKR GHDIAALAEL LGEKAGGEAA RYVHLGLTSY DVVDTAWAII IREAVRIVKA
RVKHIIKILS KLAKEYVDVP VVGRTHGQHA SPVTLGFKLA NYVYELARRY EALCDVEKRV
VKAKIGGSVG TLAFWTLLWG VEKALALRKK VAEKLGLEPH VITTQVAPRE ALAELACQLA
SLAGVLERFA LEVRELSRPE IGEWVEAPLG RVGSSAMPHK ANPVVSERIC GLSRITRGLV
VPALENIALW HERDLTNSSA ERVWIPHMLL TIDQMLVDTI ELLEKRLRFN LDAMKRNLEL
TRGHALSEAV VALLVSKGMA RHEAHRLVMS VSREAYERGE PLVEALLRNP VVARLVTRDE
LEKVLRPEGF VGAYRALVEE ALSYAEKTIS KC
//
