PUR8_PSEAE
ID PUR8_PSEAE Reviewed; 456 AA.
AC Q9I0K9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=PA2629;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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 (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; AE004091; AAG06017.1; -; Genomic_DNA.
DR PIR; F83317; F83317.
DR RefSeq; NP_251319.1; NC_002516.2.
DR RefSeq; WP_003113371.1; NZ_QZGE01000008.1.
DR PDB; 7T24; X-ray; 1.45 A; A=1-456.
DR PDB; 7T29; X-ray; 1.50 A; A=1-456.
DR PDBsum; 7T24; -.
DR PDBsum; 7T29; -.
DR AlphaFoldDB; Q9I0K9; -.
DR SMR; Q9I0K9; -.
DR STRING; 287.DR97_5333; -.
DR PaxDb; Q9I0K9; -.
DR PRIDE; Q9I0K9; -.
DR EnsemblBacteria; AAG06017; AAG06017; PA2629.
DR GeneID; 882336; -.
DR KEGG; pae:PA2629; -.
DR PATRIC; fig|208964.12.peg.2751; -.
DR PseudoCAP; PA2629; -.
DR HOGENOM; CLU_025566_2_0_6; -.
DR InParanoid; Q9I0K9; -.
DR OMA; TQVNPCD; -.
DR PhylomeDB; Q9I0K9; -.
DR BioCyc; PAER208964:G1FZ6-2669-MON; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000002438; 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; 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_0000287829"
FT ACT_SITE 171
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT ACT_SITE 296
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 248
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 297
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 302..304
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 310
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 336
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 341..345
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:7T24"
FT TURN 11..16
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:7T24"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 29..49
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:7T24"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:7T24"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7T24"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:7T24"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 180..200
FT /evidence="ECO:0007829|PDB:7T24"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:7T24"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 253..281
FT /evidence="ECO:0007829|PDB:7T24"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 306..328
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 347..365
FT /evidence="ECO:0007829|PDB:7T24"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 372..380
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:7T29"
FT HELIX 417..425
FT /evidence="ECO:0007829|PDB:7T24"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 431..438
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:7T24"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:7T24"
SQ SEQUENCE 456 AA; 50501 MW; 08648476573C398F CRC64;
MQLSSLTAVS PVDGRYAGKT SSLRPIFSEY GLIRFRVMVE VRWLQRLAAH AGIPEVAPFS
AEANALLDSL ASDFQLEHAE RIKEIERTTN HDVKAVEYLL KEQAAKLPEL AAVSEFIHFA
CTSEDINNLS HALMLREGRD SVLLPLMRQI AEAIRELAVK LADVPMLSRT HGQPASPTTL
GKELANVVYR LERQIKQVAG IELLGKINGA VGNYNAHLSA YPEVDWEANA RQFIEGDLGL
TFNPYTTQIE PHDYIAELFD AIARFNTILI DFDRDVWGYI SLGYFKQKTV AGEIGSSTMP
HKVNPIDFEN SEGNLGIANA LFQHLASKLP ISRWQRDLTD STVLRNLGVG IAHSIIAYEA
SLKGIGKLEL NAQRIAEDLD ACWEVLAEPV QTVMRRYGVE NPYEKLKELT RGKGISAEAL
QTFIEELAIP AEAKVELKKL TPAGYVGNAA AQAKRI
