ID A0A241V635_9GAMM Unreviewed; 593 AA.
AC A0A241V635;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OTG69705.1};
GN ORFNames=B9T38_14730 {ECO:0000313|EMBL:OTG69705.1};
OS Acinetobacter sp. ANC 4218.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977880 {ECO:0000313|EMBL:OTG69705.1, ECO:0000313|Proteomes:UP000194947};
RN [1] {ECO:0000313|EMBL:OTG69705.1, ECO:0000313|Proteomes:UP000194947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4218 {ECO:0000313|EMBL:OTG69705.1,
RC ECO:0000313|Proteomes:UP000194947};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-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}.
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:OTG69705.1}.
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DR EMBL; NEGD01000017; OTG69705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241V635; -.
DR STRING; 1977880.B9T38_14730; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000194947; Unassembled WGS sequence.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PF12806; Acyl-CoA_dh_C; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF12418; AcylCoA_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}.
FT DOMAIN 4..27
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 39..158
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 163..271
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 468..584
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 593 AA; 64614 MW; 3B1E4574F76BFDF7 CRC64;
MPIYNAPLAD MKFILNDVFN AEQFWQNNEN LAHVDAATAE AILEEMAKFA QNVTLPLNRT
GDEEGATYSN GNVTTPAGFK EAFKQYAEGG WIGLGADAEW GGQEMPKMLT VLSDEMLFAT
NPSFMLYPLL SVGAGMALNS YASQEQKETY LPKIYSGEWS GTMCLTEPHA GTDLGIIKTK
AERNEDGTYN ITGTKIFITG GDHDLAENII HLVLAKTPDA PAGSRGISLF IVPKFLVNED
GSLGERNHAG PGSIEHKMGI KASATCVMNF DGAKGYLVGK ENEGLAAMFV MMNYERLSMG
IQGLGASEFA YQNAAQYATD RLQGRSASGV KSPNKVADSI LVHGDVRRML LNARANNEAS
RAFAVYVGQQ LDITKFSTDA EAVKKANDRV ALLTPIAKAY LTDTAFNATL DAQMVFGGHG
FIREWGMEQC IRDLRISQIY EGTNGVQSQD LIGRKTIKCG GAFIAEYIQE IRDFANGLDA
DLNFIKDATL DAAAEVESVT QYILQASKEN IDFSNAAAVD YLHAVGLLSF SYMFAKIANA
AKAKDGEFYQ NKLSLALYFV QRILPELAMR ITKVKAGAEV VMNFSEDYFT NQA
//
