ID V9VQ69_9RHOB Unreviewed; 567 AA.
AC V9VQ69;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AHC99828.1};
GN ORFNames=METH_03035 {ECO:0000313|EMBL:AHC99828.1};
OS Leisingera methylohalidivorans DSM 14336.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHC99828.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHC99828.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHC99828.1,
RC ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) 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; CP006773; AHC99828.1; -; Genomic_DNA.
DR RefSeq; WP_024088918.1; NC_023135.1.
DR AlphaFoldDB; V9VQ69; -.
DR STRING; 999552.METH_03035; -.
DR KEGG; lmd:METH_03035; -.
DR PATRIC; fig|999552.6.peg.604; -.
DR HOGENOM; CLU_018204_12_2_5; -.
DR OrthoDB; 9807883at2; -.
DR Proteomes; UP000018780; 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; 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..33
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 81..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..439
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 451..560
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 567 AA; 60058 MW; C17D129B605C024A CRC64;
MTFRAPVSEY EFLLNHVVGY GAIPATDRFA EATPDVVSAI LNEAGKMCDE VMAPLQRNGD
LTPAFLENGV LRTSPGFGDG FKAIADGGWI GMSAPEEHGG MGLPLTVATA VNEMMAGACL
SLQLAPLMTQ GQIEALEHHA PDAIKELYLP KLISGEWSGT MNLTEPQAGS DVGALSSKAE
PNGDGTYAVS GQKIFISWGD NDFCGNICHL VLARLPDGVP GTKGISLFLV PKFLPDADGN
PGAANDLKVV SLEHKMGLHG SPTCVMQYDG ATGWLIGEEH GGMAAMFTMM NNARLGVGGQ
GVGAGEGAYQ HALAYALERK QGKTASGTIA DHADVRRMLM EMKADLFASR AILLACAQAI
DMQTATGAKD WAARAAFLTP IAKAFGTDTG IRVAETGVQV HGGMGFIEES GAAQYYRDVR
VTAIYEGTNG IQSMDLVARK MMDGGEMGFA LIDEIEEQAE RARTTHPNMA ESVWQACESL
REATEWLAAQ QDMQDRFAGS VPYLRAFARV LGGHYHLAAA MADQGGPREK LARFYITRML
PEHGSLLAHA QAGAAGAFAL TLDELAG
//
