ID A0A0H5CED5_9PSEU Unreviewed; 540 AA.
AC A0A0H5CED5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:CRK56042.1};
DE EC=1.3.8.7 {ECO:0000313|EMBL:CRK56042.1};
OS Alloactinosynnema sp. L-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK56042.1, ECO:0000313|Proteomes:UP000076116};
RN [1] {ECO:0000313|Proteomes:UP000076116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA Ramaraj T.;
RL Submitted (MAY-2015) 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; LN850107; CRK56042.1; -; Genomic_DNA.
DR RefSeq; WP_054045948.1; NZ_LN850107.1.
DR AlphaFoldDB; A0A0H5CED5; -.
DR STRING; 1653480.gene:80944901; -.
DR KEGG; alo:CRK56042; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000076116; Chromosome i.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.110.20; -; 1.
DR Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR041504; AidB_N.
DR PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42707:SF3; ACYL-COA DEHYDROGENASE AIDB-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 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|RuleBase:RU362125,
KW ECO:0000313|EMBL:CRK56042.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076116}.
FT DOMAIN 7..160
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 174..269
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 279..435
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 540 AA; 58027 MW; 55E39022D0009F55 CRC64;
MTHQVDNQAP PLTPYDAADD VALIEGLRRE GASWAEDDVR RLGKLAGGEE AQAWAEQANR
YPPELRTHDR YGNRIDEVEF HPSWHSLMRV AVVEGAASVW ADNRAGGHVA RAAGALVWGH
TEAGHGCPVS MTYAVVPALR HQPDLAAIYE PLLVSREYDP GLRIPTTKRG ILAGMGMTEK
QGGSDVRTNT TAATPTAEPG VYTLTGHKWF TSAPMCDVFL VLAQTPGGLS CFLVPRILPD
GTRNTFRIQR LKDKLGNRSN ASSEPEFDHT VAWLVGAEGR GVKTIIEMVN FTRLDCVIGT
SAIMRKALVE AGHHTRHRAA FGANLIDQPL MRNVLADLAI ESEAATTLAL RLAGAADRAV
RGDESETAFR RIATAVGKYW VTKRGPAFTA EALECLGGNG YVEESGMPRL YREAPLLSIW
EGSGNVNALD VLRALAKEPS TAEALIAELS LSTGANTHLD AAVTRLGAEL SDLEGIESRS
RRLVELMALA LQGSLLVRHA PAAVADAFCA TRLGGDWGHA FGTLPTTADV DAILTRALPH
//
