ID A0A495XB94_9PSEU Unreviewed; 398 AA.
AC A0A495XB94;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=(2S)-methylsuccinyl-CoA dehydrogenase {ECO:0000313|EMBL:RKT70606.1};
GN ORFNames=DFJ66_3876 {ECO:0000313|EMBL:RKT70606.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT70606.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT70606.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT70606.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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:RKT70606.1}.
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DR EMBL; RBXR01000001; RKT70606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495XB94; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000272729; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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; 2.
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:UP000272729}.
FT DOMAIN 11..122
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 126..228
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 242..391
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 398 AA; 43708 MW; 553C2DF58A66E233 CRC64;
MARLAQTAGL TDIQEEILST VRTFVDKEII PHAQALEHGD TYPADIVEGM KEMGLFGLTI
PEEFGGLGES LLTYALVVEQ IARGWMSVSG VINTHFIVAH MLKQHGTDEQ KQKYLPRMAT
GEVRGSFSMS EPELGSDVAA IRTRAVREGD EFVINGQKMW LTNGGTSNLT AVLVRTDEGA
DKPHQNLTTF LVEKPEGYGE VLPGLTIPGK IDKMGYKGVD TTEMVFDGFR ISPEQVLGGQ
TGQGFRHMMD GVEVGRVNVA ARACGIAIRS FELAIEYAQQ RKTFGKPIVE HQAIAFKLAE
MATKVEAAHL MMVNAARLKD SGARNDVEAG MAKLIASEYC AEVTQEAFRI HGGYGYSKEY
EIERLMREAP FLLIGEGTSE IQKTIISRGL LRDYQSRG
//
