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Database: UniProt
Entry: J9SA49_9ACTN
LinkDB: J9SA49_9ACTN
Original site: J9SA49_9ACTN 
ID   J9SA49_9ACTN            Unreviewed;       389 AA.
AC   J9SA49;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Acyl-[acyl-carrier-protein] dehydrogenase MbtN {ECO:0000256|ARBA:ARBA00040394};
DE   AltName: Full=Mycobactin synthase protein N {ECO:0000256|ARBA:ARBA00042660};
GN   ORFNames=KTR9_0547 {ECO:0000313|EMBL:AFR47213.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR47213.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR47213.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR47213.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
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.
CC       {ECO:0000256|ARBA:ARBA00037085}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005102}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP002907; AFR47213.1; -; Genomic_DNA.
DR   RefSeq; WP_014925249.1; NC_018581.1.
DR   AlphaFoldDB; J9SA49; -.
DR   STRING; 337191.KTR9_0547; -.
DR   KEGG; gor:KTR9_0547; -.
DR   PATRIC; fig|337191.3.peg.750; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_1_11; -.
DR   Proteomes; UP000003281; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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_sf.
DR   PANTHER; PTHR48083:SF20; LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
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; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN          16..127
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          131..226
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          239..387
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   389 AA;  42470 MW;  8427B80C30624666 CRC64;
     MTSTVNRPAA RSVYEPEHEA FRDSFRRFLD AEVVPGYEGW EREGLIPREL FTRAGSHGFL
     GMSVDEEFGG GGTDDFRFNA IIAEEVADAG VMSFGINLHN DICVPYFERY ADSEQKKRWL
     PGLVSGELIA AIAMTEPGTG SDLAGISTTA TLDGDHYVLN GSKTFISNGI NADLIIVAAR
     TENDGDRHGG LSLLVVERDT PGFRRGRNLD KIGMHAQDTA ELFFDDARIP KENLLGERGA
     GFRALVTNLP QERLTIAVAS TAAAGRAIEL AREYVSTRTA FGKPLSANQN TRFTLADAYV
     QTEVVRAFVD DCLSQHTTGD LTADRAAMAK LAATEVQGRV ADRCLQMFGG YGFMAEYPIA
     KAYVDARVQR IYGGANEIMK EIIGKSLFR
//
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