PUR8_THEMA
ID PUR8_THEMA Reviewed; 431 AA.
AC Q9X0I0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Adenylosuccinate lyase;
DE Short=ASL;
DE EC=4.3.2.2 {ECO:0000250|UniProtKB:P0AB89};
DE AltName: Full=Adenylosuccinase;
DE Short=ASase;
GN Name=purB; OrderedLocusNames=TM_1095;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=10673438; DOI=10.1016/s0969-2126(00)00092-7;
RA Toth E.A., Yeates T.O.;
RT "The structure of adenylosuccinate lyase, an enzyme with dual activity in
RT the de novo purine biosynthetic pathway.";
RL Structure 8:163-174(2000).
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:0000250|UniProtKB:P0AB89}.
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:P0AB89};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854;
CC Evidence={ECO:0000250|UniProtKB:P0AB89};
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:P0AB89};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921;
CC Evidence={ECO:0000250|UniProtKB:P0AB89};
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:0000269|PubMed:10673438}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD36171.1; -; Genomic_DNA.
DR PIR; A72294; A72294.
DR RefSeq; NP_228901.1; NC_000853.1.
DR RefSeq; WP_004080360.1; NZ_CP011107.1.
DR PDB; 1C3C; X-ray; 1.80 A; A/B=2-430.
DR PDB; 1C3U; X-ray; 2.30 A; A/B=1-431.
DR PDBsum; 1C3C; -.
DR PDBsum; 1C3U; -.
DR AlphaFoldDB; Q9X0I0; -.
DR SMR; Q9X0I0; -.
DR STRING; 243274.THEMA_08870; -.
DR EnsemblBacteria; AAD36171; AAD36171; TM_1095.
DR KEGG; tma:TM1095; -.
DR eggNOG; COG0015; Bacteria.
DR InParanoid; Q9X0I0; -.
DR OMA; ASSCEKI; -.
DR OrthoDB; 347727at2; -.
DR BRENDA; 4.3.2.2; 6331.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR EvolutionaryTrace; Q9X0I0; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IBA:GO_Central.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IBA:GO_Central.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.275.10; -; 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 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 1: Evidence at protein level;
KW 3D-structure; Lyase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..431
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000137886"
FT ACT_SITE 141
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:10673438"
FT ACT_SITE 262
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 4..5
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 67..69
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 93..94
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 212
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 263
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 268..270
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 307..311
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 16..36
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:1C3C"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 94..130
FT /evidence="ECO:0007829|PDB:1C3C"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1C3C"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1C3C"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 150..174
FT /evidence="ECO:0007829|PDB:1C3C"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:1C3C"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 217..243
FT /evidence="ECO:0007829|PDB:1C3C"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1C3C"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 304..333
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 338..345
FT /evidence="ECO:0007829|PDB:1C3C"
FT TURN 346..350
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 354..363
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:1C3C"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:1C3C"
FT HELIX 421..426
FT /evidence="ECO:0007829|PDB:1C3C"
SQ SEQUENCE 431 AA; 49873 MW; D3ACB25D87582869 CRC64;
MVERYSLSPM KDLWTEEAKY RRWLEVELAV TRAYEELGMI PKGVTERIRN NAKIDVELFK
KIEEKTNHDV VAFVEGIGSM IGEDSRFFHY GLTSSDVLDT ANSLALVEAG KILLESLKEF
CDVLWEVANR YKHTPTIGRT HGVHAEPTSF GLKVLGWYSE MKRNVQRLER AIEEVSYGKI
SGAVGNYANV PPEVEEKALS YLGLKPEPVS TQVVPRDRHA FYLSTLAIVA AGIERIAVEI
RHLQRTEVLE VEEPFRKGQR GSSAMPHKKN PITCERLTGL SRMMRAYVDP SLENIALWHE
RDISHSSVER YVFPDATQTL YYMIVTATNV VRNMKVNEER MKKNIDLTKG LVFSQRVLLK
LIEKGLTRKE AYDIVQRNAL KTWNSEKHFL EYLLEDEEVK KLVTKEELEE LFDISYYLKH
VDHIFERFEK E
