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Database: UniProt
Entry: P0AB89
LinkDB: P0AB89
Original site: P0AB89 
ID   PUR8_ECOLI              Reviewed;         456 AA.
AC   P0AB89; P25739;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   26-NOV-2014, entry version 89.
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=b1131, JW1117;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-6.
RC   STRAIN=K12;
RX   PubMed=1729205;
RA   He B., Smith J.M., Zalkin H.;
RT   "Escherichia coli purB gene: cloning, nucleotide sequence, and
RT   regulation by purR.";
RL   J. Bacteriol. 174:130-136(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Green S.M., Drabble W.T.;
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-456.
RC   STRAIN=K12;
RX   PubMed=1729240;
RA   Kasahara M., Nakata A., Shinagawa H.;
RT   "Molecular analysis of the Escherichia coli phoP-phoQ operon.";
RL   J. Bacteriol. 174:492-498(1992).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94 AND LYS-366, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS ALA-171 AND ASN-171
RP   IN COMPLEX WITH AMP; FUMARATE
RP   AND 2-[9-(3,4-DIHYDROXY-5-PHOSPHONOOXYMETHYL-TETRAHYDRO-FURAN-2-YL)-
RP   9H-PURIN-6-YLAMINO]-SUCCINIC ACID, ACTIVE SITE, MUTAGENESIS OF HIS-171
RP   AND SER-295, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=17531264; DOI=10.1016/j.jmb.2007.04.052;
RA   Tsai M., Koo J., Yip P., Colman R.F., Segall M.L., Howell P.L.;
RT   "Substrate and product complexes of Escherichia coli adenylosuccinate
RT   lyase provide new insights into the enzymatic mechanism.";
RL   J. Mol. Biol. 370:541-554(2007).
CC   -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
CC       {ECO:0000269|PubMed:17531264}.
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       {ECO:0000269|PubMed:17531264}.
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. {ECO:0000269|PubMed:17531264}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M74924; AAA92731.1; -; Genomic_DNA.
DR   EMBL; X59307; CAA41996.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74215.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35953.1; -; Genomic_DNA.
DR   PIR; S19212; S19212.
DR   RefSeq; NP_415649.1; NC_000913.3.
DR   RefSeq; YP_489399.1; NC_007779.1.
DR   PDB; 2PTQ; X-ray; 2.00 A; A/B=1-456.
DR   PDB; 2PTR; X-ray; 1.85 A; A/B=1-456.
DR   PDB; 2PTS; X-ray; 2.00 A; A=1-456.
DR   PDBsum; 2PTQ; -.
DR   PDBsum; 2PTR; -.
DR   PDBsum; 2PTS; -.
DR   ProteinModelPortal; P0AB89; -.
DR   SMR; P0AB89; 2-456.
DR   DIP; DIP-10608N; -.
DR   IntAct; P0AB89; 11.
DR   MINT; MINT-1253735; -.
DR   STRING; 511145.b1131; -.
DR   PaxDb; P0AB89; -.
DR   PRIDE; P0AB89; -.
DR   EnsemblBacteria; AAC74215; AAC74215; b1131.
DR   EnsemblBacteria; BAA35953; BAA35953; BAA35953.
DR   GeneID; 12933853; -.
DR   GeneID; 945695; -.
DR   KEGG; ecj:Y75_p1101; -.
DR   KEGG; eco:b1131; -.
DR   PATRIC; 32117511; VBIEscCol129921_1178.
DR   EchoBASE; EB1290; -.
DR   EcoGene; EG11314; purB.
DR   eggNOG; COG0015; -.
DR   HOGENOM; HOG000252916; -.
DR   InParanoid; P0AB89; -.
DR   KO; K01756; -.
DR   OMA; PANYIGN; -.
DR   OrthoDB; EOG686NDB; -.
DR   PhylomeDB; P0AB89; -.
DR   BioCyc; EcoCyc:ASL-MONOMER; -.
DR   BioCyc; ECOL316407:JW1117-MONOMER; -.
DR   BioCyc; MetaCyc:ASL-MONOMER; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   EvolutionaryTrace; P0AB89; -.
DR   PRO; PR:P0AB89; -.
DR   Genevestigator; P0AB89; -.
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; IDA:EcoCyc.
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   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
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   PANTHER; PTHR11444; PTHR11444; 1.
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; Acetylation; Complete proteome;
KW   Direct protein sequencing; Lyase; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    456       Adenylosuccinate lyase.
FT                                /FTId=PRO_0000137878.
FT   REGION       15     16       Substrate binding.
FT   REGION       90     92       Substrate binding.
FT   REGION      122    123       Substrate binding.
FT   REGION      301    303       Substrate binding.
FT   REGION      340    344       Substrate binding.
FT   ACT_SITE    171    171       Proton donor/acceptor.
FT                                {ECO:0000269|PubMed:17531264}.
FT   ACT_SITE    295    295       Proton donor/acceptor.
FT                                {ECO:0000269|PubMed:17531264}.
FT   BINDING     247    247       Substrate.
FT   BINDING     309    309       Substrate.
FT   BINDING     335    335       Substrate.
FT   BINDING     340    340       Substrate. {ECO:0000250}.
FT   MOD_RES      94     94       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:18723842}.
FT   MOD_RES     366    366       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:18723842}.
FT   MUTAGEN     171    171       H->A,N: Reduces catalytic activity about
FT                                500-fold. {ECO:0000269|PubMed:17531264}.
FT   MUTAGEN     295    295       S->A: Reduces catalytic activity about
FT                                1000-fold. {ECO:0000269|PubMed:17531264}.
FT   CONFLICT    145    145       P -> A (in Ref. 1; AAA92731).
FT                                {ECO:0000305}.
FT   CONFLICT    154    154       I -> L (in Ref. 1; AAA92731).
FT                                {ECO:0000305}.
FT   TURN          5      7       {ECO:0000244|PDB:2PTR}.
FT   TURN         11     16       {ECO:0000244|PDB:2PTR}.
FT   HELIX        17     19       {ECO:0000244|PDB:2PTR}.
FT   HELIX        21     25       {ECO:0000244|PDB:2PTR}.
FT   HELIX        29     49       {ECO:0000244|PDB:2PTR}.
FT   HELIX        61     72       {ECO:0000244|PDB:2PTR}.
FT   HELIX        76     89       {ECO:0000244|PDB:2PTR}.
FT   HELIX        92    104       {ECO:0000244|PDB:2PTR}.
FT   HELIX       108    111       {ECO:0000244|PDB:2PTR}.
FT   HELIX       112    116       {ECO:0000244|PDB:2PTR}.
FT   TURN        117    120       {ECO:0000244|PDB:2PTR}.
FT   HELIX       123    141       {ECO:0000244|PDB:2PTR}.
FT   HELIX       143    160       {ECO:0000244|PDB:2PTR}.
FT   TURN        161    163       {ECO:0000244|PDB:2PTR}.
FT   STRAND      165    170       {ECO:0000244|PDB:2PTR}.
FT   STRAND      173    179       {ECO:0000244|PDB:2PTR}.
FT   HELIX       180    200       {ECO:0000244|PDB:2PTR}.
FT   HELIX       215    220       {ECO:0000244|PDB:2PTR}.
FT   HELIX       226    236       {ECO:0000244|PDB:2PTR}.
FT   STRAND      246    248       {ECO:0000244|PDB:2PTR}.
FT   HELIX       252    280       {ECO:0000244|PDB:2PTR}.
FT   STRAND      283    286       {ECO:0000244|PDB:2PTR}.
FT   HELIX       305    327       {ECO:0000244|PDB:2PTR}.
FT   HELIX       338    342       {ECO:0000244|PDB:2PTR}.
FT   HELIX       343    345       {ECO:0000244|PDB:2PTR}.
FT   HELIX       346    366       {ECO:0000244|PDB:2PTR}.
FT   STRAND      367    369       {ECO:0000244|PDB:2PTR}.
FT   HELIX       371    378       {ECO:0000244|PDB:2PTR}.
FT   HELIX       382    385       {ECO:0000244|PDB:2PTR}.
FT   HELIX       386    395       {ECO:0000244|PDB:2PTR}.
FT   HELIX       401    407       {ECO:0000244|PDB:2PTR}.
FT   HELIX       416    424       {ECO:0000244|PDB:2PTR}.
FT   STRAND      426    428       {ECO:0000244|PDB:2PTR}.
FT   HELIX       430    437       {ECO:0000244|PDB:2PTR}.
FT   HELIX       441    443       {ECO:0000244|PDB:2PTR}.
FT   HELIX       448    454       {ECO:0000244|PDB:2PTR}.
SQ   SEQUENCE   456 AA;  51543 MW;  8D1F4546B66795BC CRC64;
     MELSSLTAVS PVDGRYGDKV SALRGIFSEY GLLKFRVQVE VRWLQKLAAH AAIKEVPAFA
     ADAIGYLDAI VASFSEEDAA RIKTIERTTN HDVKAVEYFL KEKVAEIPEL HAVSEFIHFA
     CTSEDINNLS HALMLKTARD EVILPYWRQL IDGIKDLAVQ YRDIPLLSRT HGQPATPSTI
     GKEMANVAYR MERQYRQLNQ VEILGKINGA VGNYNAHIAA YPEVDWHQFS EEFVTSLGIQ
     WNPYTTQIEP HDYIAELFDC VARFNTILID FDRDVWGYIA LNHFKQKTIA GEIGSSTMPH
     KVNPIDFENS EGNLGLSNAV LQHLASKLPV SRWQRDLTDS TVLRNLGVGI GYALIAYQST
     LKGVSKLEVN RDHLLDELDH NWEVLAEPIQ TVMRRYGIEK PYEKLKELTR GKRVDAEGMK
     QFIDGLALPE EEKARLKAMT PANYIGRAIT MVDELK
//
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