PUR8_STAAW
ID PUR8_STAAW Reviewed; 431 AA.
AC Q7A0G9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=MW1849;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH AMP AND OXALATE, AND
RP SUBUNIT.
RC STRAIN=ATCC 35556;
RX PubMed=20693687; DOI=10.1107/s0907444910020081;
RA Fyfe P.K., Dawson A., Hutchison M.T., Cameron S., Hunter W.N.;
RT "Structure of Staphylococcus aureus adenylosuccinate lyase (PurB) and
RT assessment of its potential as a target for structure-based inhibitor
RT discovery.";
RL Acta Crystallogr. D 66:881-888(2010).
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: Homodimer and homotetramer. Residues from neighboring subunits
CC contribute catalytic and substrate-binding residues to each active
CC site. {ECO:0000269|PubMed:20693687}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000033; BAB95714.1; -; Genomic_DNA.
DR RefSeq; WP_000572878.1; NC_003923.1.
DR PDB; 2X75; X-ray; 2.50 A; A=1-431.
DR PDBsum; 2X75; -.
DR AlphaFoldDB; Q7A0G9; -.
DR SMR; Q7A0G9; -.
DR EnsemblBacteria; BAB95714; BAB95714; BAB95714.
DR KEGG; sam:MW1849; -.
DR HOGENOM; CLU_030949_0_1_9; -.
DR OMA; ASSCEKI; -.
DR BRENDA; 4.3.2.2; 3352.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR EvolutionaryTrace; Q7A0G9; -.
DR Proteomes; UP000000418; 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; 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.
FT CHAIN 1..431
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000259978"
FT ACT_SITE 141
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
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 276
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 8..13
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 16..36
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:2X75"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 94..130
FT /evidence="ECO:0007829|PDB:2X75"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2X75"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:2X75"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 150..175
FT /evidence="ECO:0007829|PDB:2X75"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 217..244
FT /evidence="ECO:0007829|PDB:2X75"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:2X75"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:2X75"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 304..333
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 338..344
FT /evidence="ECO:0007829|PDB:2X75"
FT TURN 345..350
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:2X75"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:2X75"
FT TURN 368..375
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 389..393
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:2X75"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:2X75"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:2X75"
SQ SEQUENCE 431 AA; 49603 MW; 493F79CBE814B9E5 CRC64;
MIERYSREEM SNIWTDQNRY EAWLEVEILA CEAWSELGHI PKADVQKIRQ NAKVNVERAQ
EIEQETRHDV VAFTRQVSET LGEERKWVHY GLTSTDVVDT ALSFVIKQAN DIIEKDLERF
IDVLAEKAKN YKYTLMMGRT HGVHAEPTTF GVKMALWYTE MQRNLQRFKQ VREEIEVGKM
SGAVGTFANI PPEIESYVCK HLGIGTAPVS TQTLQRDRHA YYIATLALIA TSLEKFAVEI
RNLQKTETRE VEEAFAKGQK GSSAMPHKRN PIGSENITGI SRVIRGYITT AYENVPLWHE
RDISHSSAER IMLPDVTIAL DYALNRFTNI VDRLTVFEDN MRNNIDKTFG LIFSQRVLLA
LINKGMVREE AYDKVQPKAM ISWETKTPFR ELIEQDESIT SVLTKEELDE CFDPKHHLNQ
VDTIFERAGL A
