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Database: UniProt
Entry: A0A165KLT3_9BURK
LinkDB: A0A165KLT3_9BURK
Original site: A0A165KLT3_9BURK 
ID   A0A165KLT3_9BURK        Unreviewed;       386 AA.
AC   A0A165KLT3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=A1D30_08865 {ECO:0000313|EMBL:KZT15675.1};
OS   Acidovorax sp. GW101-3H11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT15675.1, ECO:0000313|Proteomes:UP000077219};
RN   [1] {ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA   Ray J., Price M., Deutschbauer A.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KZT15675.1, ECO:0000313|Proteomes:UP000077219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT15675.1,
RC   ECO:0000313|Proteomes:UP000077219};
RX   PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA   Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA   Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA   Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA   Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT   "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL   Nature 557:503-509(2018).
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   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005102}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZT15675.1}.
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DR   EMBL; LUKZ01000009; KZT15675.1; -; Genomic_DNA.
DR   RefSeq; WP_063460012.1; NZ_LUKZ01000009.1.
DR   AlphaFoldDB; A0A165KLT3; -.
DR   STRING; 1813946.A1D30_08865; -.
DR   OrthoDB; 9770681at2; -.
DR   Proteomes; UP000077219; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          9..118
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          235..383
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  42632 MW;  1F855721F3C12092 CRC64;
     MIERTLFQPE HQAFADSFRR FIEKEVTPHH ADWEDQGYVA REVWSQAGAN GFLCMSLPEE
     YGGAGADKLY SVAQMEELAR AGTTGIGFGL HSEIVAPYIL HYGTEEQKRK YLPQMASGAV
     VGAIAMSEPA AGSDLQGIKT TAIKSADGSH YVLNGSKTFI TNGWHADLVI VVAKTDPAAG
     AKGTSLLLVE RGMPGFEKGQ RLKKLGMKAQ DTSELFFNDV KVPAENLLGG PAMEGRGFIC
     LMEQLPWERL QIAITAVAAA QAAIDWTLDY VKERKVFGQP VASFQNTRYT LAELQTEVQV
     ARVFVDKCCE LIARDQLDTQ TASMAKYWTT DLQCKVMDEC VQMFGGYGYM WEYPITRAYA
     DARVQRIYGG TNEIMKEVIS RGMGLK
//
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