位置:首页 > 蛋白库 > PUR8_STAAS
PUR8_STAAS
ID   PUR8_STAAS              Reviewed;         431 AA.
AC   Q6G825;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SAS1831;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(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: Homodimer and homotetramer. Residues from neighboring subunits
CC       contribute catalytic and substrate-binding residues to each active site
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571857; CAG43636.1; -; Genomic_DNA.
DR   RefSeq; WP_000572878.1; NC_002953.3.
DR   AlphaFoldDB; Q6G825; -.
DR   SMR; Q6G825; -.
DR   KEGG; sas:SAS1831; -.
DR   HOGENOM; CLU_030949_0_1_9; -.
DR   OMA; ASSCEKI; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
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   3: Inferred from homology;
KW   Lyase; Purine biosynthesis.
FT   CHAIN           1..431
FT                   /note="Adenylosuccinate lyase"
FT                   /id="PRO_0000259976"
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"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024