ID A0A0T5NVI8_9RHOB Unreviewed; 384 AA.
AC A0A0T5NVI8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Name=mmgC_27 {ECO:0000313|EMBL:QEW29744.1};
GN ORFNames=RIdsm_05590 {ECO:0000313|EMBL:QEW29744.1}, XM52_28085
GN {ECO:0000313|EMBL:KRS12953.1};
OS Roseovarius indicus.
OG Plasmid pRIdsm_01 {ECO:0000313|EMBL:QEW29744.1}, and
OG Plasmid pridsm_01 {ECO:0000313|Proteomes:UP000325785}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS12953.1, ECO:0000313|Proteomes:UP000051401};
RN [1] {ECO:0000313|EMBL:KRS12953.1, ECO:0000313|Proteomes:UP000051401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B108 {ECO:0000313|EMBL:KRS12953.1,
RC ECO:0000313|Proteomes:UP000051401};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius indicus B108T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEW29744.1, ECO:0000313|Proteomes:UP000325785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW29744.1,
RC ECO:0000313|Proteomes:UP000325785};
RC PLASMID=pridsm_01 {ECO:0000313|Proteomes:UP000325785}, and pRIdsm_01
RC {ECO:0000313|EMBL:QEW29744.1};
RA Vollmers J., Petersen J.;
RT "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT geographic distances.";
RL Submitted (AUG-2018) 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 ---------------------------------------------------------------------------
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; LAXI01000040; KRS12953.1; -; Genomic_DNA.
DR EMBL; CP031599; QEW29744.1; -; Genomic_DNA.
DR RefSeq; WP_057821778.1; NZ_LAXI01000040.1.
DR AlphaFoldDB; A0A0T5NVI8; -.
DR STRING; 540747.SAMN04488031_12913; -.
DR KEGG; rid:RIdsm_05590; -.
DR PATRIC; fig|540747.5.peg.4746; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000051401; Unassembled WGS sequence.
DR Proteomes; UP000325785; Plasmid pridsm_01.
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 ECO:0000313|EMBL:QEW29744.1}; Plasmid {ECO:0000313|EMBL:QEW29744.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051401}.
FT DOMAIN 14..112
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 125..219
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 230..379
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 384 AA; 42029 MW; 7B408A44D056B4AB CRC64;
MTEKRRRPAE TVDRVMFRDT CRRFAEREIA PIWEEADRES QFSRAFFTAA ANAGLIGIAA
PAEVGGAGLG VHEEAICIEE CARINPGLPN ALIIQGVAGG ILHDFGTAEQ KELARASIEG
DKILAIAVTE PDAGNDVQNV KTAARRDGDD WKLDGIKSFI TLAGESDVLV LLAQTDPARG
RDGMSFFAVD RRSPGVEVSR IPTYANRPAP TYRVHLDHVR VPEARRVPAG FRQIMMGFNR
ERILVSARWS GHMQHAQDWA LDYAKTRHQF GRPIGANQSI AFKLAQNQTD IEAARLLTYQ
AADRWDSGCP IADLIQQVSC AKLFVTQAVV RVTQSALHIG GGWGLTEELP VMRMALDALV
APVTVGSFEI QLRAIAKQLG LPCD
//
