ID U7U857_9BURK Unreviewed; 591 AA.
AC U7U857;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N879_16650 {ECO:0000313|EMBL:ERT55049.1};
OS Alcaligenes sp. EGD-AK7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERT55049.1, ECO:0000313|Proteomes:UP000016497};
RN [1] {ECO:0000313|EMBL:ERT55049.1, ECO:0000313|Proteomes:UP000016497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERT55049.1};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ERT55049.1}.
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DR EMBL; AVOG02000069; ERT55049.1; -; Genomic_DNA.
DR RefSeq; WP_022983613.1; NZ_AVOG02000069.1.
DR AlphaFoldDB; U7U857; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000016497; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016497}.
FT DOMAIN 40..159
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 165..272
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 283..454
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 486..584
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 591 AA; 65181 MW; 28879E3E7231C4FA CRC64;
MQASHYQPPL EDFRFVQQYC LQAEEDWCRL SAYEGLDQET ADRVVEAAGR FCADVLAPLN
GPADLQGCRL ENGRVLTPDG FAKAYTDFVA AGWPALACDP GVGGQGLPQL LDTALHEMLA
SANHGWAMYP GILHGAYACL NAHGDEYIRR TYLPHIVSGR WLATMCLTEP QAGSDLGLLR
TQALPEQEGS YRLHGNKIFI SGGDQDMSEN IVHLVLARLP DAPAGTRGLS LFLAPRLIPK
EGGLVPNTIY CDGLEKKMGI KGSATCSMRF EAAHAWLIGK PHQGLAAMFV MMNSARLHVG
LQGLGHAEAA WQLARSYAHE RYQMRVQPRP AQANGVADPI AHHPAMQRIL ADLRVWTEGM
RVMAAWTAHQ LDLAQSLPEG EEQTRAQDLA SLLTPVVKSL FTERGFSLAS DALQVFGGYG
YVHEYRIEQT LRDARIAMIY EGTNQIQALD LLQRKIAAVG PEALQPLLQA WRWEADACLE
ALAECPWGKA LRQWSDQLYI VTTHLCTCAQ HDTQVLARCA EDYLRLVGIV CMAFAWARAG
RVSRLHADTS LCERKVASAD YFFDHGLLDA RYYLSRIEAA VTSAVPVHKL V
//
