ID U7U8Q8_9BURK Unreviewed; 781 AA.
AC U7U8Q8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Acyl-coenzyme A dehydrogenase {ECO:0000256|ARBA:ARBA00020144};
DE EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033};
DE EC=1.3.8.8 {ECO:0000256|ARBA:ARBA00012040};
GN ORFNames=N879_19900 {ECO:0000313|EMBL:ERT55715.1};
OS Alcaligenes sp. EGD-AK7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERT55715.1, ECO:0000313|Proteomes:UP000016497};
RN [1] {ECO:0000313|EMBL:ERT55715.1, ECO:0000313|Proteomes:UP000016497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERT55715.1};
RX PubMed=24407646;
RA Sagarkar S., Bhardwaj P., Yadav T.C., Qureshi A., Khardenavis A.,
RA Purohit H.J., Kapley A.;
RT "Draft genome sequence of atrazine-utilizing bacteria isolated from Indian
RT agricultural soil.";
RL Genome Announc. 2:e01149-13(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC ChEBI:CHEBI:83726; EC=1.3.8.7;
CC Evidence={ECO:0000256|ARBA:ARBA00034035};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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:ERT55715.1}.
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DR EMBL; AVOG02000009; ERT55715.1; -; Genomic_DNA.
DR RefSeq; WP_022983328.1; NZ_AVOG02000009.1.
DR AlphaFoldDB; U7U8Q8; -.
DR OrthoDB; 9802447at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000016497; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; 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; 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 InterPro; IPR015396; FadE_C.
DR PANTHER; PTHR48083:SF18; ACYL-COENZYME A DEHYDROGENASE; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF09317; ACDH_C; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000016497}.
FT DOMAIN 81..192
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 320..467
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 474..762
FT /note="Acyl-CoA dehydrogenase C-terminal bacterial-type"
FT /evidence="ECO:0000259|Pfam:PF09317"
SQ SEQUENCE 781 AA; 86098 MW; 07DE12839F1305C0 CRC64;
MFVTLLLIVL VLGCVYVLKN RNLRTKWLSR PIYRAFSSVL PAMSQTERDA LEAGTVWWES
ELFRGKPNWN TLSSYPAYRL TDEERQFMDN EVNVACAMID DWQVSQEDFD MPAEVWNYLK
ENRFFSLIIP KEYGGRGFSA QAHSAVVAKL STRNSALSVS VMVPNSLGPA ELLLHYGTDE
QKQHYLPRLA DGRDIPAFAL TSPWAGSDAA SIPDVGIVCK GEWEGQEVLG MRVTWDKRYI
TLAPVCTLLG LAFRLYDPDG LLGGEKDIGI TCALVPSDHP GVDTGRRHFP LNAMFMNGPT
RGKDVFMPLE FIIGGPAMAG QGWRMLMECL AAGRSISLPS SFTGMAKLTS RAVGGYSAVR
TQFRSAISKF EGVEEALARI AGHTYAMDAA RTMTAAAVDL GEKPSVVSAI VKYHVTERGR
IVVNDGMDVI GGKGICLGPS NFLGRAYQQI PVGITVEGAN ILTRSLIIFG QGAIRCHPFI
LEEMTAALNP DREAGLRKFD QAFWAHIRYT LANTGRSFWL GLGGWRLLSG PTGTSKAMHT
YYSQASRYSA AFSLLADASM LVLGGSLKMR ERLSSRLGDV LSELYMLSAV LKRYQDEGRH
QEDAPLAHWA AQDALMRAQH ALDKVLENFP NRPLAAVLRF LVFPLGLRRL GPDDKLDHTV
AKLLTKPGAT RDRLTYDTYL PDDDMEPVGA IEAALLASLN TRDIDAKIRQ FEKSGQLQDN
PKANVRDLAE AVFQAGGITA QEYEQIQARD IVRDRVIAVD DFPFDLRREN PAAEAASGSQ
A
//
