PUR8_LEGPH
ID PUR8_LEGPH Reviewed; 456 AA.
AC Q5ZXD1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=lpg0801;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE017354; AAU26889.1; -; Genomic_DNA.
DR RefSeq; WP_010946537.1; NC_002942.5.
DR RefSeq; YP_094836.1; NC_002942.5.
DR PDB; 3BHG; X-ray; 1.90 A; A=1-456.
DR PDBsum; 3BHG; -.
DR AlphaFoldDB; Q5ZXD1; -.
DR SMR; Q5ZXD1; -.
DR STRING; 272624.lpg0801; -.
DR PaxDb; Q5ZXD1; -.
DR PRIDE; Q5ZXD1; -.
DR EnsemblBacteria; AAU26889; AAU26889; lpg0801.
DR GeneID; 66489982; -.
DR KEGG; lpn:lpg0801; -.
DR PATRIC; fig|272624.6.peg.828; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_025566_2_0_6; -.
DR OMA; TQVNPCD; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR EvolutionaryTrace; Q5ZXD1; -.
DR Proteomes; UP000000609; 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; 1.10.275.10; -; 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 InterPro; IPR013539; PurB_C.
DR Pfam; PF08328; ASL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
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..456
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000349271"
FT ACT_SITE 171
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT ACT_SITE 295
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 15..16
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 90..92
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 122..123
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 247
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 296
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 301..303
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 309
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 335
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 340..344
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3BHG"
FT TURN 11..16
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3BHG"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 29..48
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:3BHG"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:3BHG"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:3BHG"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:3BHG"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3BHG"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 180..200
FT /evidence="ECO:0007829|PDB:3BHG"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:3BHG"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 252..280
FT /evidence="ECO:0007829|PDB:3BHG"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 305..327
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 346..364
FT /evidence="ECO:0007829|PDB:3BHG"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 371..379
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 416..424
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 430..438
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:3BHG"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:3BHG"
SQ SEQUENCE 456 AA; 51403 MW; 9470797DE25CFE03 CRC64;
MTLTALNAIS PIDGRYVNKT RALSPYFSEF ALTYYRLMVE IKWFESLAAN DTIPEVPALD
NKARKFLSDL ISNFNESEAE KIKEFEKQTN HDVKAVEYYL QDKFQENEQL KSCVAFIHFA
CTSEDINNLA YALMIKQAIA QVIQPTIAEI MGSITLLGKQ HADVAMLSRT HGQPATPTTM
GKELVNFVAR LKRPQQQLAE VLIPAKFNGA VGNYNAHVAA YPEVDWRKHC ANFVTSLGLS
FNAYTTQIEP HDGIAEVSQI MVRINNILLD YTQDIWSYIS LGYFKQKTIA EEVGSSTMPH
KVNPIDFENA EGNLGLSNAL FIHFANKLTQ SRMQRDLSDS TVLRNLGVAF SYSLIAYHSV
AKGNDKLQIN KSALQKDLSE NWEVLAEAIQ TVMRRYNEPN AYEQLKELTR GQMIDAENLK
KFIKTLSIPE EAKAELMKLT PETYTGLATQ LVKAFS
