ID   DDAG_ENTAG              Reviewed;         396 AA.
AC   E2JA32;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Fumarate--(S)-2,3-diaminopropanoate ligase {ECO:0000305};
DE            EC=6.3.2.46 {ECO:0000269|PubMed:19807062};
DE   AltName: Full=ATP-dependent fumaroyl-DAP ligase {ECO:0000303|PubMed:19807062};
GN   Name=ddaG {ECO:0000303|PubMed:19807062};
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].
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-dependent
RT   epoxidation by DdaC during dapdiamide antibiotic biosynthesis.";
RL   J. Am. Chem. Soc. 132:15773-15781(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND 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 fumaramoyl-
RT   dipeptide scaffold of the dapdiamide antibiotics.";
RL   Biochemistry 48:10467-10472(2009).
CC   -!- FUNCTION: Involved in dapdiamide antibiotics biosynthesis. Ligates
CC       fumarate and 2,3-diaminopropionate (DAP) to form N-beta-fumaroyl-DAP.
CC       Can also form N-succinoyl-DAP from succinate and DAP, with lower
CC       efficiency. {ECO:0000269|PubMed:19807062}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-diaminopropanoate + ATP + fumarate = AMP + diphosphate
CC         + N(3)-fumaroyl-(S)-2,3-diaminopropanoate; Xref=Rhea:RHEA:44340,
CC         ChEBI:CHEBI:29806, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57721, ChEBI:CHEBI:84330, ChEBI:CHEBI:456215;
CC         EC=6.3.2.46; Evidence={ECO:0000269|PubMed:19807062};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.55 mM for fumarate {ECO:0000269|PubMed:19807062};
CC         KM=20 mM for succinate {ECO:0000269|PubMed:19807062};
CC         Note=kcat is 11.6 sec(-1) with fumarate as substrate. kcat is 3.8
CC         sec(-1) with succinate as substrate. {ECO:0000269|PubMed:19807062};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:19807062}.
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DR   EMBL; HQ130277; ADN39487.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2JA32; -.
DR   SMR; E2JA32; -.
DR   KEGG; ag:ADN39487; -.
DR   BioCyc; MetaCyc:MON-19475; -.
DR   BRENDA; 6.3.2.46; 2084.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR042099; ANL_N_sf.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Ligase.
FT   CHAIN           1..396
FT                   /note="Fumarate--(S)-2,3-diaminopropanoate ligase"
FT                   /id="PRO_0000434793"
SQ   SEQUENCE   396 AA;  44753 MW;  F39AB59FCE643F5A CRC64;
     MNKGENMNLE MWVQNISATF PWYAQLLRDK QADLSRLESL PLITEELLTQ HYYHAENSFP
     GEHHSYLTSG TTSGKRKRIF YSDNDQRIYL QQRMDIIRDF CGEGHTRACA DLGTGHAAAT
     AGEIFQAMGC DVELIDFTRP IEQHIEVLNR FKPDIFFTMP MILDSLIATG KLDFQPKRII
     LLGDVASLNW QNKVADYFHI QPAQVLDLFG SIEIGSIAFY NHAQKRYQFD SYVRPEVVPV
     QSLYPGAKYG GDGGILLLTS FAREYFPAVR FVTNDLIEGF AQENVGGRTV YTYQRCLGRF
     AGEFKHGEKI NLSDISDALA NNLPYHKYDL ADHEGGLVIR IAAKSIPTEV IEAIKHDLLA
     RNPDIAQMIS SGLVGDIRIQ CVDAQEITGN VSKRRY