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Database: UniProt
Entry: O28041
LinkDB: O28041
Original site: O28041 
ID   PUR8_ARCFU              Reviewed;         444 AA.
AC   O28041;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-OCT-2013, entry version 97.
DE   RecName: Full=Adenylosuccinate lyase;
DE            Short=ASL;
DE            EC=4.3.2.2;
DE   AltName: Full=Adenylosuccinase;
DE            Short=ASase;
GN   Name=purB; OrderedLocusNames=AF_2242;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
OS   9628 / NBRC 100126).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
CC   -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-
CC       (5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 2/2.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC   -!- SUBUNIT: Homotetramer. Residues from neighboring subunits
CC       contribute catalytic and substrate-binding residues to each active
CC       site (By similarity).
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily.
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DR   EMBL; AE000782; AAB89013.1; -; Genomic_DNA.
DR   PIR; B69530; B69530.
DR   RefSeq; NP_071067.1; NC_000917.1.
DR   ProteinModelPortal; O28041; -.
DR   STRING; 224325.AF2242; -.
DR   EnsemblBacteria; AAB89013; AAB89013; AF_2242.
DR   GeneID; 1485473; -.
DR   KEGG; afu:AF2242; -.
DR   eggNOG; COG0015; -.
DR   KO; K01756; -.
DR   OMA; TNSANER; -.
DR   ProtClustDB; PRK08540; -.
DR   BioCyc; AFUL224325:GJBC-2289-MONOMER; -.
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 AMP-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   PANTHER; PTHR11444; PTHR11444; 1.
DR   PANTHER; PTHR11444:SF2; PTHR11444:SF2; 1.
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   Complete proteome; Lyase; Purine biosynthesis; Reference proteome.
FT   CHAIN         1    444       Adenylosuccinate lyase.
FT                                /FTId=PRO_0000137887.
FT   REGION        9     10       Substrate binding (By similarity).
FT   REGION       73     75       Substrate binding (By similarity).
FT   ACT_SITE    145    145       Proton donor/acceptor (By similarity).
FT   ACT_SITE    269    269       Proton donor/acceptor (By similarity).
FT   BINDING     219    219       Substrate (By similarity).
FT   BINDING     308    308       Substrate (By similarity).
FT   BINDING     313    313       Substrate (By similarity).
FT   BINDING     317    317       Substrate (By similarity).
SQ   SEQUENCE   444 AA;  50758 MW;  A0F919725D4B813D CRC64;
     MIVHPIDYRY GTPEMKRIWS EDSKIKRMVR VEMALLRALA KKGYLSEEEA KEAKKKAYSV
     TPERVKEIEA EIKHDIMALV KAITEATGCR WVHFGATSND IIDTATALQL RDSLKILEVK
     IKRLAKVLAD KALEYKDVVC LGRTHGQAAL PTTYGFRFAL WAAEVARHYI RLQQMKDRLL
     VGQMSGAVGT QAAFGKDGFE IEEEVMRLLN LKPALISSQI IPRDSYCEYL EFLANLAATL
     EKIALNFRLL QRAEVGELME KFEAKQVGSS TMPHKRNPID CENVCGLARV VRGFVEPQHQ
     SAILWEERDL TNSSAERITL VESTVLADHI LTKMIKVVSS VSLNLENIRR NLEMQRGLNL
     SEAVMIEMTK RGVGRQEAHE ILRQAAMRAY ENNSSLLDEL LKDERVMKYF KEDELREILK
     PENYLGTARE RVERVVRWVN EVLK
//
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