ID A0A0J7LHC3_9FLAO Unreviewed; 595 AA.
AC A0A0J7LHC3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KMQ68400.1};
GN ORFNames=ACM39_07725 {ECO:0000313|EMBL:KMQ68400.1};
OS Chryseobacterium sp. FH2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1674291 {ECO:0000313|EMBL:KMQ68400.1, ECO:0000313|Proteomes:UP000036315};
RN [1] {ECO:0000313|EMBL:KMQ68400.1, ECO:0000313|Proteomes:UP000036315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH2 {ECO:0000313|EMBL:KMQ68400.1,
RC ECO:0000313|Proteomes:UP000036315};
RA Stropko S.J., Miller J.R., Newman J.D.;
RL Submitted (JUN-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}.
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:KMQ68400.1}.
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DR EMBL; LFNE01000004; KMQ68400.1; -; Genomic_DNA.
DR RefSeq; WP_048510466.1; NZ_LFNE01000004.1.
DR AlphaFoldDB; A0A0J7LHC3; -.
DR STRING; 1674291.ACM39_07725; -.
DR PATRIC; fig|1674291.3.peg.1612; -.
DR OrthoDB; 9802867at2; -.
DR Proteomes; UP000036315; Unassembled WGS sequence.
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}.
FT DOMAIN 30..142
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 147..245
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 257..419
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 470..568
FT /note="Acyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21263"
SQ SEQUENCE 595 AA; 65707 MW; F66C051AD59FEB24 CRC64;
MTTLNKTLKG GEFLIKEIPA NEIFSLEELS EEQKMLRDSA KEFIDREVVP QKERFEKKDY
AFTEETMRKL GEMGLLGIAV PEEYGGLGMG FVTTMLACDY ISGTTGSLAT AYGAHTGIGT
LPIVLYGTEA QKQKYLPDLA TGTKFGAYCL TEPDAGSDAN SGKTRAKLSE DGKHYIINGQ
KMWISNAGFA DTFTLFAKID DDKNITGFVI NRSELENPES LTFGEEEHKL GIRASSTRQV
FFNDMKIPVE NLLGERNNGF KIALNALNVG RIKLAAACLD AQRRILNHSI QYSNERKQFG
VSISTFGAIR KKIAEMATGT FVSESGSYRA AKNVEDKINE LVADGLSHQE AELKGVEEFA
VECSILKVFV SDLAQNTADE GIQVYGGMGF SEDTPMEAAW RDSRISRIYE GTNEINRLLA
VGMLIKRAMK GELDLLSPAM AISKELMGIP SFEVPDYSAF MSEEKAIIAN LKKVFLMVSG
AALQKYMMDI EKQQHLLLNA SEILNQIYMA ESAVLRAEKH FSPDSVEAAM AQLNLYKAVE
KIISAAKEGI ISFAEGDEQR MMLSGLRRFT KYTNNPNVVA LTEKVAAHYI NKGAY
//
