ID A0A291GGV6_9RHOB Unreviewed; 516 AA.
AC A0A291GGV6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ATG49425.1};
GN ORFNames=CEW89_18690 {ECO:0000313|EMBL:ATG49425.1};
OS Celeribacter ethanolicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1758178 {ECO:0000313|EMBL:ATG49425.1, ECO:0000313|Proteomes:UP000217935};
RN [1] {ECO:0000313|EMBL:ATG49425.1, ECO:0000313|Proteomes:UP000217935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSPH2 {ECO:0000313|EMBL:ATG49425.1,
RC ECO:0000313|Proteomes:UP000217935};
RA Woo J.-H., Kim H.-S.;
RT "Celeribacter sp. TSPH2 complete genome sequence.";
RL Submitted (JUN-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}.
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DR EMBL; CP022196; ATG49425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GGV6; -.
DR STRING; 1758178.GCA_001550095_02451; -.
DR KEGG; ceh:CEW89_18690; -.
DR OrthoDB; 7801364at2; -.
DR Proteomes; UP000217935; 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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000217935}.
FT DOMAIN 69..151
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 156..256
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 267..422
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 516 AA; 55088 MW; 98B2892B82722FC4 CRC64;
MTPFKAPLDD ILFCLRHVAG ADRLPEWDAE LAEGILGHFA SFAEGVIAPL DEPGDAQGCT
LSEGRVTMPD GFKDAYTQLA EGGWQGLTAP EEFGGMGQNA LLAAGVSEIF SGANHAMQMV
CNLVPGAIST LMKFGSDAQK QHWIPRLAAG ETLSTMCLTE PGAGSDLSRI RTKATPSGDS
WRIEGEKIFI SGGDQDMSED VLHLVLARTG GDGVKGLSLF LCPSEVEGTR NAVTVTRIEE
KLGLHASPTC QLAFDGAEAE LIGDEGAGLM AMFTMMNHAR LDVSLQGVAH ASRAYHIAAD
YAAERKQGRK ADGTEALLAD HPDVQRMLDE QKSLALGARA MTYLTMAELT LGQNRALVDF
LTPICKVFCT EAGIHAADLG IQVLGGYGYL TEYRVSQTWR DARITSIYEG ANGIHAVALA
TRGLRAAEGP EAFAKLVEEL ASGDPDCLSL LSEWQDARAG MAEQAVEKAH DFMALTGEVL
FRAVWCKLAA TGAAEMIRLA KRVARRPLPV RLPLSA
//
