ID   DDAD_ENTAG              Reviewed;         578 AA.
AC   E2JA29;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Dapdiamide synthesis protein DdaD {ECO:0000305};
GN   Name=ddaD {ECO:0000303|PubMed:20945916};
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, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, PATHWAY, AND PHOSPHOPANTETHEINYLATION AT SER-533.
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).
CC   -!- FUNCTION: Involved in dapdiamide antibiotics biosynthesis. Activates
CC       and sequesters N-beta-fumaramoyl-DAP as a covalently tethered thioester
CC       for subsequent oxidative modification of the fumaramoyl group.
CC       {ECO:0000269|PubMed:20945916}.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000269|PubMed:20945916};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=420 uM for N-beta-fumaramoyl-DAP {ECO:0000269|PubMed:20945916};
CC         Note=kcat is 64 min(-1). {ECO:0000269|PubMed:20945916};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:20945916}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; HQ130277; ADN39483.1; -; Genomic_DNA.
DR   RefSeq; WP_033781250.1; NZ_JPOT02000004.1.
DR   AlphaFoldDB; E2JA29; -.
DR   SMR; E2JA29; -.
DR   BioCyc; MetaCyc:MON-19478; -.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..578
FT                   /note="Dapdiamide synthesis protein DdaD"
FT                   /id="PRO_0000434794"
FT   DOMAIN          498..573
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         533
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT                   ECO:0000269|PubMed:20945916"
SQ   SEQUENCE   578 AA;  64048 MW;  4A7D07F2FFCDF99C CRC64;
     MHSVETFNLP ALNSLLETTA RRFGNRLAVQ DDNGSLTFAD FVEKVGILSA KLRLVIKRGE
     HVAVQLPRGI NYIVAAYAIW EAGGVYLPLD NQWPSSRIEG ILHRSHVRVL IHTSQADQGL
     ELTELPAETR AESPVAGTPA YIIHTSGTTG EPKGVVVSHE SLIHLVESHQ RDIYQAYDVT
     EGPVAINASF CFDSALERMA LVALGYSLHV VSDQVRKSPY ELVKYLRDNS IVNVDLVPSH
     LKVLLSAGLN EKCDALRLVI VGGEAIDAEL WREIVQNQAI YINVYGPTEN TINTSFCEIR
     GETPHIGRPF KNVTCLLLNE NGERCAAGEE GELLVAGRHL AQGYYNAPDL TDRVFVHIDG
     IRYYRTGDRV RQNEQGNLLY LGRIDDQVKI NGFRIELADV QHNLTQLPGV KYAAVTPIKL
     PTGQGLLASI VWNSDAPEQT FSNLEALLGE KLPSYMVPTR WQKLDALPLT DNLKLDHKSL
     LSHWKNSQEQ IGEKFAAESI SATEHQIKNL WQKILRQPSL SPDAHFFASG GDSMAAMTLL
     VELKKVTPQD VSLGDIFKYP TIRKMAAWLD ASSVQAES