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Database: UniProt
Entry: A0A1X0H380_9MYCO
LinkDB: A0A1X0H380_9MYCO
Original site: A0A1X0H380_9MYCO 
ID   A0A1X0H380_9MYCO        Unreviewed;       433 AA.
AC   A0A1X0H380;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ORB20713.1};
GN   ORFNames=BST36_19020 {ECO:0000313|EMBL:ORB20713.1};
OS   Mycolicibacterium moriokaense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=39691 {ECO:0000313|EMBL:ORB20713.1, ECO:0000313|Proteomes:UP000192354};
RN   [1] {ECO:0000313|EMBL:ORB20713.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP105393 {ECO:0000313|EMBL:ORB20713.1};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (FEB-2017) 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:ORB20713.1}.
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DR   EMBL; MVIB01000019; ORB20713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0H380; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000192354; 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}.
FT   DOMAIN          9..130
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          134..212
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          247..396
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   433 AA;  48536 MW;  08043CD9E24A5FD6 CRC64;
     MAWDFETDPE YQKVLDWADE FVRQEVEPLD LAFPHQQFVP LEGKRRDAVD PLKDEVRKRG
     LWATHLGPEL GGQGYGQLKL ALLNEILGRS QWAPIVFGCQ APDTGNAEII AHYGTEEQKQ
     KYLMPLLNGE LFSCYSMTEP HAGADPTLFK TRAVRDGDDW VINGWKFFSS NARTASFLIV
     MAVTNPDVSA YQGMSMFLVP TDTPGVNIVR DIGLYGEPEG QGGHALIHYE NVRVPAEALL
     GGEGQAFVIA QTRLGGGRIH HAMRTIGLAQ RALDMMCERA LSRQTQGSRL SDKQFVQGYI
     ADSYAQLLQF RLMVLYTAWE IDKYNDYKKV RKDISAVKVA MPTVLHDIAW RAMQVHGALG
     VTNEMPFMGM VTGAAVMGLA DGPTEVHKTT VAKQVLRDYQ ATEDTWPTEW TPRKREEART
     KYADFLEHQV GNL
//
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