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Database: UniProt
Entry: G8RYM8_MYCRN
LinkDB: G8RYM8_MYCRN
Original site: G8RYM8_MYCRN 
ID   G8RYM8_MYCRN            Unreviewed;       433 AA.
AC   G8RYM8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AEV74481.1};
GN   OrderedLocusNames=MycrhN_3972 {ECO:0000313|EMBL:AEV74481.1};
OS   Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV74481.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV74481.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV74481.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) 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}.
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DR   EMBL; CP003169; AEV74481.1; -; Genomic_DNA.
DR   RefSeq; WP_014212233.1; NC_016604.1.
DR   AlphaFoldDB; G8RYM8; -.
DR   STRING; 710685.MycrhN_3972; -.
DR   KEGG; mrh:MycrhN_3972; -.
DR   PATRIC; fig|710685.3.peg.3987; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_1_0_11; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000005442; Chromosome.
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:UP000005442}.
FT   DOMAIN          9..130
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          134..211
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;  48313 MW;  8BCA9D33700F359A CRC64;
     MAWDFETDPE YQKVLDWADE FVREEVEPLD LAFPHLQFTP LEGKRRDAID PLKEEVRRRG
     LWATHLGPEL GGQGYGQLKL ALLNEILGRS QWAPIVFGCQ APDTGNAEII AHYGTDEQKQ
     KYLMPLLGGE LFSCYSMTEP HAGADPTLFT TSAVRDGDDW VINGHKFFSS NASTASFLIV
     MVVTNPDVSA YQGMSMFLVP TDTPGVNIIR NVGLYGEPEG QGSHALIHYD NVRVPAEALL
     GGEGQAFVIA QTRLGGGRIH HAMRTIGMSQ RALDMMCERA LSRETQGSRL SDKQFVQGYI
     ADSYAQLLQF RLMVLYTAWE IDKYNDYKKV RKDIAAVKVA MPTVLHDIAW RAMQVHGALG
     VTNEMPFLGM VTGAAVMGLA DGPTEVHKTT VAKQVLRDYR PTDDTWPTEW EPRKREAARA
     KYADYLENEV GNL
//
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