ID A0A159Z0K3_9RHOB Unreviewed; 566 AA.
AC A0A159Z0K3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AMY67404.1};
GN ORFNames=AKL17_0142 {ECO:0000313|EMBL:AMY67404.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY67404.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY67404.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-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; CP012661; AMY67404.1; -; Genomic_DNA.
DR RefSeq; WP_066808599.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A159Z0K3; -.
DR STRING; 1335048.AKL17_0142; -.
DR KEGG; daa:AKL17_0142; -.
DR PATRIC; fig|1335048.3.peg.149; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000076128; 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; IPR025878; Acyl-CoA_dh-like_C_dom.
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 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 78..156
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..269
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 281..432
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 448..559
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 566 AA; 59928 MW; FE3319BE1D2E2CD6 CRC64;
MPYRSPVGEF RFILDQVVPL APVAATERFA EATGETVDAI LTEAGRMCDE VLAPLQRNGD
LHPARLENGV LRSSPGFAEG YAAIAEGGWV GLAAPQEFGG MGLPQALNMA VNDMMSGACL
ALQLNPLLTQ GQIEALEHHA SDELKALYLP KLISGEWSGT MNLTEPQAGS DVGAVRSKAD
PNGDGTYAIT GQKIFISWGD SDVTANVCHL VLARLPDAAP GTRGISLFMV PKYIPDADGA
PGARNSLKVV SLEHKMGLHG SPTCVMAFEG ATGWMVGGEA KGMAAMFTMM NNARLAVGVQ
GIGVAEAAYQ KALDYALDRK QMGAIIEHAD VRRMLAGMKA DIFAARSIAL ACAVALDMGR
ATGEPEWQAR AALLTPIAKA FGTDVGMAVS ETGVQIHGGM GFVEETGAAQ FYRDVRVTAI
YEGTNGIQAM DLVGRKMMDG GEAAFRLLQE VEDAANMARA ARPELADLAE QVWTAAETLR
EATEWLVRQE VQDRFAGAVP YLRAFARVLG AHFHLKAALA EAEAGPRAAL ARIYVTRLLP
QFAAALDEAR QGAEGLYALS AEDLAA
//
