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Database: UniProt
Entry: K0JWN6_SACES
LinkDB: K0JWN6_SACES
Original site: K0JWN6_SACES 
ID   K0JWN6_SACES            Unreviewed;       389 AA.
AC   K0JWN6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00019125};
GN   OrderedLocusNames=BN6_18790 {ECO:0000313|EMBL:CCH29199.1};
OS   Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS   15066 / NRRL 15764).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH29199.1, ECO:0000313|Proteomes:UP000006281};
RN   [1] {ECO:0000313|EMBL:CCH29199.1, ECO:0000313|Proteomes:UP000006281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC   {ECO:0000313|Proteomes:UP000006281};
RX   PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA   Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA   Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT   "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT   comparison to the other completely sequenced Pseudonocardiaceae.";
RL   BMC Genomics 13:465-465(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; HE804045; CCH29199.1; -; Genomic_DNA.
DR   RefSeq; WP_015099312.1; NC_019673.1.
DR   AlphaFoldDB; K0JWN6; -.
DR   STRING; 1179773.BN6_18790; -.
DR   KEGG; sesp:BN6_18790; -.
DR   PATRIC; fig|1179773.3.peg.1886; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_3_5_11; -.
DR   OrthoDB; 8876745at2; -.
DR   BioCyc; SESP1179773:BN6_RS09230-MONOMER; -.
DR   Proteomes; UP000006281; 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:SF2; MEDIUM-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; 3.
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, 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:UP000006281}.
FT   DOMAIN          7..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..378
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   389 AA;  43338 MW;  1F6F970049D93117 CRC64;
     MDFTLDDEQK EIRDWVRTFV RKEVVPLEPE VLRRERAGQP GLGRDELKAL QDKAKAAGFF
     GVLTPREYGG MGLGAVMTAL VEQELGRSFV PFRFGGYADN ILFHGNEEQK RRYLLPTISG
     ERVSCFAITE PGAGSDAKAI RTSARKEGGE WVVNGEKTFI TQGHEADFVM VFAVTDKEKG
     AAGGVTCFLV DREMGWKSEP IPTMGQWGPA ALVFDDVRVP EANVLGEVGQ GFRLAMQWIG
     QGRYLLPARA LGACERLVEM AVEQAKNRVA FGQPIAEYQA IQWMLADSAV EVEALRWLVL
     HAAWLVDQGA DSRQAQSIAK LYGGIKANEI VDRVLQIHGG MGYTRELPIE RWYRELRLLR
     IYEGTDEIQR RTIARNLLRG HAKVTGTLG
//
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