ID   MBTN_MYCSS              Reviewed;         389 AA.
AC   Q1BBA3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Mmcs_1722;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000384; ABG07831.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1BBA3; -.
DR   SMR; Q1BBA3; -.
DR   KEGG; mmc:Mmcs_1722; -.
DR   HOGENOM; CLU_709451_0_0_11; -.
DR   OMA; MMTRRQF; -.
DR   BioCyc; MSP164756:G1G6O-1763-MON; -.
DR   UniPathway; UPA00011; -.
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; IPR013786; AcylCoA_DH/ox_N.
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   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..389
FT                   /note="Acyl-[acyl-carrier-protein] dehydrogenase MbtN"
FT                   /id="PRO_0000278307"
SQ   SEQUENCE   389 AA;  42009 MW;  818F901CFF82FB0F CRC64;
     MTLAAHTTED YEELLGRVFD DQVKAWTAEA EASERFPRQL IEHLGRTGVF TQKWGDGQQP
     DVAKLIALAL ELGRLGSAGI GVGVSLHDSA IALLRRFAKN DYLRTICEQA IRGEAVLCIG
     ASEISGGSDL QIVGTEVRSV RDGYEVRGVK KFVSLSPIAD HIMVVARNVD HDPGSRHGNV
     VVIAVPTSQV EAQAPYRKVG AGPLDTAAVH IDTWVPGDAL IARPGTGLAA ISWGLAHERL
     SIAGQVAGAS QRVIGITLAR MMKRRQFGHT LYEHQALRMR MADLQARVDM LRYALAGIAA
     GGRLDLRAAA AIKVTAARLG EEVLSECMHI FGGSGYLTDE TPLGRWWRDM KLARVGGGTD
     EVLWELVAAA MRPDYDGYDE LIDSPTGDD