ID A0A073BAT9_9PSEU Unreviewed; 382 AA.
AC A0A073BAT9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=GU90_06605 {ECO:0000313|EMBL:KEI44894.1};
OS Saccharopolyspora rectivirgula.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=28042 {ECO:0000313|EMBL:KEI44894.1, ECO:0000313|Proteomes:UP000031419};
RN [1] {ECO:0000313|EMBL:KEI44894.1, ECO:0000313|Proteomes:UP000031419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43113 {ECO:0000313|EMBL:KEI44894.1,
RC ECO:0000313|Proteomes:UP000031419};
RA Barrera C., Millon L., Rognon B., Zaugg C., Monod M.;
RT "Saccharopolyspora rectivirgula DSM-43113 Genome sequencing.";
RL Submitted (JUN-2014) 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.
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}.
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:KEI44894.1}.
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DR EMBL; JNVU01000017; KEI44894.1; -; Genomic_DNA.
DR RefSeq; WP_029722105.1; NZ_JNVU01000017.1.
DR AlphaFoldDB; A0A073BAT9; -.
DR STRING; 28042.GU90_06605; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9769473at2; -.
DR Proteomes; UP000031419; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; 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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF37; ACYL-COA DEHYDROGENASE; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031419}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 122..214
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 227..374
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 382 AA; 41583 MW; 0A571BF6C9CC3AEC CRC64;
MDFNLTADQQ RRRDAARKFA EQQLAPGYRR REQQGGIEPR IRIQMGQSGF IAPEVPPTYG
GRGLDRLTSG MLVEEISRGD FSVAYLQVVG SLVAQVLVEN ATPELAASWV PKICAGEEVV
GIGLTEPHAG SDAANPHLRA RRDGDEYVLD GTKSLSFAAE AAAAVVFART DEQQSGSKGI
SAFLVPLDLP GVTRGPYSDM GTKAVGRGAV HFQRTRIPAD HLLGREGEGF SQVMKGFDFS
RALIGLQCLG AAQVTVDETW EHVTRRQAFG QPLSKFQGVS FPLAEAETVL SAARLLCYQT
LWLKDQGAPH TAQAAMCKWW APKTAFEVIQ DCLLLHGQYG YRTDLPIEQR LRDVLGLQIG
DGTAQIMKLV VARQRVGRAL AP
//
