ID A5V0T7_ROSS1 Unreviewed; 394 AA.
AC A5V0T7;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:ABQ92490.1};
DE EC=1.3.8.1 {ECO:0000313|EMBL:ABQ92490.1};
GN OrderedLocusNames=RoseRS_4146 {ECO:0000313|EMBL:ABQ92490.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ92490.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) 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; CP000686; ABQ92490.1; -; Genomic_DNA.
DR AlphaFoldDB; A5V0T7; -.
DR STRING; 357808.RoseRS_4146; -.
DR KEGG; rrs:RoseRS_4146; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_0; -.
DR Proteomes; UP000006554; Chromosome.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR CDD; cd01158; SCAD_SBCAD; 1.
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; 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; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 21..132
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 137..231
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 244..392
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 394 AA; 42933 MW; 9F3645BF523A5498 CRC64;
MMGRESGASH KGGNGMDFAL SDQHEMLRQT VRAFAEQEIR PTAAARDEAM EFPVDLVKKM
GQLGLMGVAV SEQYGGAGLD YISYAIVIEE LSRVDASLGV IASVNNSLVC YGIETFGTEE
QKRELLTPLA SGRMLGAFSL SEPGAGSDAA AQKTTAVRDG DEYVINGIKN WVTNGDYADT
IILMAMTDPS RGHRGITAFL VDPHAPGCSI VKVEHKLGIR SAHSCQMAYD NYRVPAWRRL
GEEGQGFKIA MTILNAGRIG IAAQAVGIAQ GAYEAALEYA KIREQFGKPI IENQAIGFTL
ADMATRIKAA RLLTYEAAWR KDQHLDFVSA ASMAKLYASE TAMWTATKAV QVFGSNGYSK
EYPVERYFRD AKITEIYEGT SEIQRLVIAR EIAR
//
