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Database: UniProt
Entry: A0A0A6UCD6_ACTUT
LinkDB: A0A0A6UCD6_ACTUT
Original site: A0A0A6UCD6_ACTUT 
ID   A0A0A6UCD6_ACTUT        Unreviewed;       401 AA.
AC   A0A0A6UCD6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KHD72733.1};
GN   ORFNames=MB27_40745 {ECO:0000313|EMBL:KHD72733.1};
OS   Actinoplanes utahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1869 {ECO:0000313|EMBL:KHD72733.1, ECO:0000313|Proteomes:UP000054537};
RN   [1] {ECO:0000313|EMBL:KHD72733.1, ECO:0000313|Proteomes:UP000054537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 12052 {ECO:0000313|EMBL:KHD72733.1,
RC   ECO:0000313|Proteomes:UP000054537};
RA   Velasco-Bucheli B., del Cerro C., Hormigo D., Garcia J.L., Acebal C.,
RA   Arroyo M., de la Mata I.;
RT   "Draft genome sequence of Actinoplanes utahensis NRRL 12052.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KHD72733.1}.
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DR   EMBL; JRTT01000137; KHD72733.1; -; Genomic_DNA.
DR   RefSeq; WP_043533442.1; NZ_JRTT01000137.1.
DR   AlphaFoldDB; A0A0A6UCD6; -.
DR   STRING; 1869.MB27_40745; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 3176804at2; -.
DR   Proteomes; UP000054537; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 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   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:UP000054537}.
FT   DOMAIN          9..125
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          129..231
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          243..392
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   401 AA;  43701 MW;  86564005CB964534 CRC64;
     MDFEFDAKTE DYRKRLLAFM DEHVYPAEAT FHTGHDGWEP PAALKGLQAA AKEAGLWNLF
     LPGEHGAGLT NLQYAPLAEI TGRSPAIAPP ALNCAAPDTG NMEVLADFGT AEQKAKWLAP
     LLNGEIRSAF AMTEPQVASS DATNISTRIQ RDGDDYVVNG RKFYITGAMN PNCKIFIVMG
     KTDPDAPRHL QQSQILVPRD TPGVTVKRGM TVLGYTDGDH GGHAEIIFED VRVPATNLIG
     EEGGGFAISQ ARLGPGRIHH CMRLIGMAER ALELMCTRAL VRTPFGKPLA EQGVVQDWIA
     ESRVRIEQSR LLVLKAAWLM DTVGNKGAHT EIQAIKIAVP STVEWIVDKA IQTHGAAGVG
     QDFPLAGLFA SARMLRLADG PDEVHKRSLA HRELKRYRSS K
//
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