GenomeNet

Database: UniProt
Entry: E2JA31
LinkDB: E2JA31
Original site: E2JA31 
ID   DDAF_ENTAG              Reviewed;         424 AA.
AC   E2JA31;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   05-DEC-2018, entry version 28.
DE   RecName: Full=Dapdiamide A synthase {ECO:0000305};
DE            EC=6.3.2.47 {ECO:0000269|PubMed:19807062, ECO:0000269|PubMed:20945916};
DE   AltName: Full=ATP-dependent N-fumaramoyl-DAP-amino acid ligase {ECO:0000303|PubMed:19807062};
GN   Name=ddaF {ECO:0000303|PubMed:19807062};
GN   Synonyms=apvF {ECO:0000312|EMBL:AFJ97210.1};
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=CU0119;
RX   PubMed=20945916; DOI=10.1021/ja1072367;
RA   Hollenhorst M.A., Bumpus S.B., Matthews M.L., Bollinger J.M. Jr.,
RA   Kelleher N.L., Walsh C.T.;
RT   "The nonribosomal peptide synthetase enzyme DdaD tethers N(beta)-
RT   fumaramoyl-l-2,3-diaminopropionate for Fe(II)/alpha-ketoglutarate-
RT   dependent epoxidation by DdaC during dapdiamide antibiotic
RT   biosynthesis.";
RL   J. Am. Chem. Soc. 132:15773-15781(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=48b/90;
RX   PubMed=23233458; DOI=10.1002/mbo3.43;
RA   Sammer U.F., Reiher K., Spiteller D., Wensing A., Volksch B.;
RT   "Assessment of the relevance of the antibiotic 2-amino-3-(oxirane-2,3-
RT   dicarboxamido)-propanoyl-valine from Pantoea agglomerans biological
RT   control strains against bacterial plant pathogens.";
RL   MicrobiologyOpen 1:438-449(2012).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   PATHWAY.
RC   STRAIN=CU0119;
RX   PubMed=19807062; DOI=10.1021/bi9013165;
RA   Hollenhorst M.A., Clardy J., Walsh C.T.;
RT   "The ATP-dependent amide ligases DdaG and DdaF assemble the
RT   fumaramoyl-dipeptide scaffold of the dapdiamide antibiotics.";
RL   Biochemistry 48:10467-10472(2009).
CC   -!- FUNCTION: Involved in dapdiamide antibiotics biosynthesis
CC       (PubMed:19807062, PubMed:20945916). Ligates N-beta-fumaramoyl-DAP
CC       and valine, isoleucine or leucine to form dapdiamides A, B or C,
CC       respectively (PubMed:19807062). Also ligates N-beta-
CC       epoxysuccinamoyl-DAP and valine to form dapdiamide E
CC       (PubMed:20945916). {ECO:0000269|PubMed:19807062,
CC       ECO:0000269|PubMed:20945916}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-[[[(2R,3R)-3-carboxyoxiran-2-yl]carbonyl]amino]-L-
CC         alanine + ATP + L-valine = ADP + dapdiamide E + H(+) +
CC         phosphate; Xref=Rhea:RHEA:45080, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:84912, ChEBI:CHEBI:84913, ChEBI:CHEBI:456216;
CC         EC=6.3.2.47; Evidence={ECO:0000269|PubMed:20945916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + N(3)-fumaramoyl-(S)-2,3-
CC         diaminopropanoate = ADP + dapdiamide A + H(+) + phosphate;
CC         Xref=Rhea:RHEA:44344, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57762, ChEBI:CHEBI:84320,
CC         ChEBI:CHEBI:84331, ChEBI:CHEBI:456216; EC=6.3.2.47;
CC         Evidence={ECO:0000269|PubMed:19807062};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-isoleucine + N(3)-fumaramoyl-(S)-2,3-
CC         diaminopropanoate = ADP + dapdiamide B + H(+) + phosphate;
CC         Xref=Rhea:RHEA:44348, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58045, ChEBI:CHEBI:84321,
CC         ChEBI:CHEBI:84331, ChEBI:CHEBI:456216; EC=6.3.2.47;
CC         Evidence={ECO:0000269|PubMed:19807062};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + N(3)-fumaramoyl-(S)-2,3-
CC         diaminopropanoate = ADP + dapdiamide C + H(+) + phosphate;
CC         Xref=Rhea:RHEA:44352, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57427, ChEBI:CHEBI:84322,
CC         ChEBI:CHEBI:84331, ChEBI:CHEBI:456216; EC=6.3.2.47;
CC         Evidence={ECO:0000269|PubMed:19807062};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Note=Binds 1 magnesium or manganese ion per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00409};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.26 mM for valine {ECO:0000269|PubMed:19807062};
CC         KM=0.83 mM for isoleucine {ECO:0000269|PubMed:19807062};
CC         KM=7.82 mM for leucine {ECO:0000269|PubMed:19807062};
CC         KM=72 uM for N-beta-fumaramoyl-DAP
CC         {ECO:0000269|PubMed:20945916};
CC         KM=53 uM for N-beta-epoxysuccinamoyl-DAP
CC         {ECO:0000269|PubMed:20945916};
CC         Note=kcat is 8.1 min(-1) with valine as substrate. kcat is 9.5
CC         min(-1) with isoleucine as substrate. kcat is 11.2 min(-1) with
CC         leucine as substrate (PubMed:19807062). kcat is 21 min(-1) with
CC         N-beta-fumaramoyl-DAP as substrate. kcat is 181 min(-1) with N-
CC         beta-epoxysuccinamoyl-DAP as substrate (PubMed:20945916).
CC         {ECO:0000269|PubMed:19807062, ECO:0000269|PubMed:20945916};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:19807062,
CC       ECO:0000269|PubMed:20945916}.
DR   EMBL; HQ130277; ADN39488.1; -; Genomic_DNA.
DR   EMBL; JQ901494; AFJ97210.1; -; Genomic_DNA.
DR   RefSeq; WP_033781244.1; NZ_JPOT02000004.1.
DR   KEGG; ag:ADN39488; -.
DR   KO; K22114; -.
DR   BioCyc; MetaCyc:MONOMER-19476; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011761; ATP-grasp.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; ATP-binding; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN         1    424       Dapdiamide A synthase.
FT                                /FTId=PRO_0000434792.
FT   DOMAIN      120    318       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     147    209       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       275    275       Magnesium or manganese.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       287    287       Magnesium or manganese.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
SQ   SEQUENCE   424 AA;  46884 MW;  F9A9BA70B5825E84 CRC64;
     MSILNNKEVI VIIDAWSGGK HLIPAFQALG YFCLHVQSTF LPEVFIADNQ LAIARSDRHI
     VHDGNIETLL SQLQPYTIKA ILAGSEGAVG LADCLNDALE LTFSNQFELS AARRNKYLMQ
     EQLALKGVAS INQQLAGHSD ELKQWLAGHA HWPVVLKPIQ SAGTDGVFIC HDLAQALQAF
     EAILAKKDFF GSPNREVLCQ EFLAGEEFVV NGIACQGEYF FTELWQSKKQ QRNGFPVYET
     QYLHYQNDAG FDVLTAYTVQ VCQTLGINNG AFHAEVMMTS GGPVLIEIGA RVAGGADPYI
     IEECLGHSQI SKLAQAVLHP AKFLQECRRQ HDFSGHRRAA YVYMISPSPG RVQVSPEEKF
     IKIDGVISIN YHYAPGDIQQ ETCDLLSSPG VIIAIRDNPA LLKQTIAEIR DVEADFYHLG
     LIDE
//
DBGET integrated database retrieval system