ID   MBTN_MYCTO              Reviewed;         386 AA.
AC   P9WQF8; L0T946; P63431; Q11016;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
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=MT1388;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45652.1; -; Genomic_DNA.
DR   PIR; A70740; A70740.
DR   RefSeq; WP_003406953.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQF8; -.
DR   SMR; P9WQF8; -.
DR   EnsemblBacteria; AAK45652; AAK45652; MT1388.
DR   GeneID; 45425324; -.
DR   KEGG; mtc:MT1388; -.
DR   PATRIC; fig|83331.31.peg.1496; -.
DR   HOGENOM; CLU_709451_0_0_11; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000001020; 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.
FT   CHAIN           1..386
FT                   /note="Acyl-[acyl-carrier-protein] dehydrogenase MbtN"
FT                   /id="PRO_0000426783"
SQ   SEQUENCE   386 AA;  41180 MW;  60A2765380F89EFB CRC64;
     MTAGSDLDDF RGLLAKAFDE RVVAWTAEAE AQERFPRQLI EHLGVCGVFD AKWATDARPD
     VGKLVELAFA LGQLASAGIG VGVSLHDSAI AILRRFGKSD YLRDICDQAI RGAAVLCIGA
     SEESGGSDLQ IVETEIRSRD GGFEVRGVKK FVSLSPIADH IMVVARSVDH DPTSRHGNVA
     VVAVPAAQVS VQTPYRKVGA GPLDTAAVCI DTWVPADALV ARAGTGLAAI SWGLAHERMS
     IAGQIAASCQ RAIGITLARM MSRRQFGQTL FEHQALRLRM ADLQARVDLL RYALHGIAEQ
     GRLELRTAAA VKVTAARLGE EVISECMHIF GGAGYLVDET TLGKWWRDMK LARVGGGTDE
     VLWELVAAGM TPDHDGYAAV VGASKA