ID A4XEQ6_NOVAD Unreviewed; 404 AA.
AC A4XEQ6;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ABP64417.1};
GN OrderedLocusNames=Saro_3557 {ECO:0000313|EMBL:ABP64417.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OG Plasmid pNL2 {ECO:0000313|EMBL:ABP64417.1,
OG ECO:0000313|Proteomes:UP000009134}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABP64417.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|EMBL:ABP64417.1, ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RC PLASMID=pNL2 {ECO:0000313|EMBL:ABP64417.1,
RC ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Han C., Thomson S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Fredrickson J., Romine M.F., Richardson P.;
RT "Complete sequence of plasmid pNL2 of Novosphingobium aromaticivorans DSM
RT 12444.";
RL Submitted (APR-2007) 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; CP000677; ABP64417.1; -; Genomic_DNA.
DR RefSeq; WP_011906804.1; NC_009427.1.
DR AlphaFoldDB; A4XEQ6; -.
DR KEGG; nar:Saro_3557; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_0_5; -.
DR Proteomes; UP000009134; Plasmid pNL2.
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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 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.
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}; Plasmid {ECO:0000313|EMBL:ABP64417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT DOMAIN 6..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..215
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 235..401
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 404 AA; 44072 MW; 064B16E3E7321505 CRC64;
MDIELSPEDQ AFRDEVRAFL AANLPREVID GAASSPTVFV EPDIGQRWNA ILAAKGWLAY
QWPKEAGGTG WSPVQRYIFE KECALAGAPN LTVLGLKLVA PVIYTFGTPE QKAKYLPRIL
SGEDYWCQGF SEPGSGSDLA SLQCRATLSE DGTHYKLNGS KIWTTHAHWA NRMFALVRTD
ATVKKQAGIS FVLVDMNQPG VSVRPLLTLA GDHEVNQVFL EDAIVPVEDR IGEEGDGWKL
AKFLLENERG GSCHSPKLEY DLGQIEKDAA AEPDGRGGRL ADDADWKRRV AKVRLGIQSL
EMIELKILSE VAKGRPPGPQ TSLCKLLASN LRQDVDLLAV DLYGTAGLQL DFARPFYGDN
APAAIHSRGA QVASARYLNS RAWTIFGGTN EVQAGIIART VLGL
//
