ID A0A0F2L800_9CREN Unreviewed; 404 AA.
AC A0A0F2L800;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=TU36_00960 {ECO:0000313|EMBL:KJR72610.1};
OS Vulcanisaeta sp. AZ3.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1609231 {ECO:0000313|EMBL:KJR72610.1, ECO:0000313|Proteomes:UP000054362};
RN [1] {ECO:0000313|EMBL:KJR72610.1, ECO:0000313|Proteomes:UP000054362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-2015) 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:KJR72610.1}.
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DR EMBL; JZWU01000014; KJR72610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2L800; -.
DR PATRIC; fig|1609231.3.peg.262; -.
DR Proteomes; UP000054362; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR CDD; cd00567; ACAD; 1.
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; 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 PIRSF; PIRSF016578; HsaA; 2.
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..128
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 134..227
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 242..395
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 404 AA; 46133 MW; 11980171314102F2 CRC64;
MSSTLDVLDL FPQYAEELKL LRKTAREFAQ RNFTPELARE YDKKEEFPWD LYRKAGELGL
LAPSVPTEYN GGGFSTYLAD IVVTEELVRA EPTLGEAIMS GTFSSHLLYF FGTEEQKRKY
LPPVYRGENT FFGAYTEPEH GTDITQLNTV AERKGDRFII RGMKTFITNA PTAKYGILLA
QTDPEKRHRG QTLFIIHTDW PGVTIRKLTG KMGQRSIPVG EIYLDNVEVP IDYVVGGEKG
INQGFYWTLA YFNISRLGPA AMALGMMLAA FDKAVEYAKK RVQFGQQIIN FQLIQEKLGR
MATLIEASRS LLYRAAYYVD DYIKFKIDPR AMAAMTSAAK VFVTDAANEV IDMAIQVFGG
YGYFEEFDVE RYWRDHRVTR IYEGTNEINL LTIVDTLRRD AWKP
//
