ID A6H0C0_FLAPJ Unreviewed; 596 AA.
AC A6H0C0;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Acyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:CAL43793.1};
DE EC=1.3.99.- {ECO:0000313|EMBL:CAL43793.1};
GN OrderedLocusNames=FP1726 {ECO:0000313|EMBL:CAL43793.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL43793.1, ECO:0000313|Proteomes:UP000006394};
RN [1] {ECO:0000313|EMBL:CAL43793.1, ECO:0000313|Proteomes:UP000006394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC {ECO:0000313|Proteomes:UP000006394};
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL43793.1; -; Genomic_DNA.
DR RefSeq; WP_011963836.1; NC_009613.3.
DR RefSeq; YP_001296600.1; NC_009613.3.
DR AlphaFoldDB; A6H0C0; -.
DR STRING; 402612.FP1726; -.
DR EnsemblBacteria; CAL43793; CAL43793; FP1726.
DR KEGG; fps:FP1726; -.
DR PATRIC; fig|402612.5.peg.1743; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_3_10; -.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 2.
DR InterPro; IPR049426; Acyl-CoA-dh-like_C.
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; PF21263; Acyl-CoA-dh_C; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 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:UP000006394}.
FT DOMAIN 27..140
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 144..238
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..413
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 464..567
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 596 AA; 65723 MW; 850CA839D4CAA017 CRC64;
MSDKTRGGQF IVKETKCEAI FTPEDFNEEQ LMMRDSVKEF VDKELWAHKD RFEKKDYAYT
QECMKKAGDL GFLSVAVPEA YGGMGMGFVN TVLVCDHISG ATGSFSTAFG AHTGIGTMPI
TLYGTEEQKQ KYVPKLASGE WFGAYCLTEP GAGSDANSGK TKAVLSEDGK TYSITGQKMW
ISNAGFCSVF IVFARIGDDK NITGFIVENT PDNGISMNEE EHKLGIRASS TRQVFFNDTK
VPAENMLSER GNGFKIAMNA LNVGRIKLAA ACLDAQRRVI TQAVNYSNER IQFNTAISQF
GAIRSKLAEM ATSCYAGESA TYRAAKDIED RITEREAAGS SHQEAELKGV EEYAIECSIL
KVAVSEDVQA CADEGIQIFG GMGFSEDTPM ESAWRDARIA RIYEGTNEIN RMLSVGMLIK
KAMKGHVDLL GPASKVQEEL MGIPSFETPD YSELFAEEKE MITKLKKAFL MVAGGAVQKY
GPDLDAHQQL LMAASDILIE IYMAESTILR TEKLAKTNGA DKVKEQIAMA QLYLYQAVDI
ITQKGKESII SFAEGDEQRM MLMGLRRFTK YTNMPNVVGL RETITTKLVA ENAYCF
//
