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 01-MAY-2013, entry version 96.
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; PVLGWTH; -.
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:EC.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA: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; IPR003031; D_crystallin.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR000362; Fumarate_lyase.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR004769; Pur_lyase.
DR PANTHER; PTHR11444:SF2; PTHR11444:SF2; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-Aspartase-like; 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
//
