ID   MBTN_MYCPA              Reviewed;         388 AA.
AC   Q73ZP8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Acyl-[acyl-carrier-protein] dehydrogenase MbtN;
DE            Short=Acyl-ACP dehydrogenase MbtN;
DE            EC=1.3.99.-;
DE   AltName: Full=Mycobactin synthase protein N;
GN   Name=mbtN; Synonyms=fadE14; OrderedLocusNames=MAP_1553c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- FUNCTION: Catalyzes the dehydrogenation at the alpha-beta position of
CC       ACP-bound acyl chains. This results in the introduction of a double
CC       bond in the lipidic chain, which is further transferred to the epsilon-
CC       amino group of lysine residue in the mycobactin core by MbtK (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE016958; AAS03870.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q73ZP8; -.
DR   SMR; Q73ZP8; -.
DR   STRING; 262316.MAP_1553c; -.
DR   EnsemblBacteria; AAS03870; AAS03870; MAP_1553c.
DR   KEGG; mpa:MAP_1553c; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_709451_0_0_11; -.
DR   OMA; MMTRRQF; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..388
FT                   /note="Acyl-[acyl-carrier-protein] dehydrogenase MbtN"
FT                   /id="PRO_0000278306"
SQ   SEQUENCE   388 AA;  41370 MW;  175382E1627F6755 CRC64;
     MSAATTADID HYRTVLAGAF DDQVLEWTRE AEARQRFPRE LIEHLGARGV FSEKWCGGML
     PDVGKLVELA RALGRLSSAG IGVGVSLHDS AIAVLRRFGK SDYLRDICER AIAGQAVLCI
     GASEESGGSD LQIVRTEMSS RDGGFDIRGV KKFVSLSPIA DHIMVVARSI DHDSASKHGN
     VALIAVPTSQ ASVQRPYAKV GAGPLDTAAV HIDTWVPADA LVARAGTGLA AISWGLAHER
     MSIAGQIAAS CQRAIGITLA RMMTRRQFGR TLFEHQALRL RMADLQARVD LLQHGLNGIA
     AQGRLDLRAA AGVKVTAARL GEEVMSECMH IFGGAGYLVE ETPLGRWWRD MKLARVGGGT
     DEVLWELVAA GMAADHGGYR SVVGASSA