ID C5T1G0_ACIDE Unreviewed; 598 AA.
AC C5T1G0;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:EER61718.1};
GN ORFNames=AcdelDRAFT_0740 {ECO:0000313|EMBL:EER61718.1};
OS Acidovorax delafieldii 2AN.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=573060 {ECO:0000313|EMBL:EER61718.1, ECO:0000313|Proteomes:UP000003856};
RN [1] {ECO:0000313|EMBL:EER61718.1, ECO:0000313|Proteomes:UP000003856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2AN {ECO:0000313|EMBL:EER61718.1,
RC ECO:0000313|Proteomes:UP000003856};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA Picardal F., Roden E., Emerson D.;
RT "The draft genome of Acidovorax delafieldii 2AN.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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:EER61718.1}.
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DR EMBL; ACQT01000011; EER61718.1; -; Genomic_DNA.
DR RefSeq; WP_005793513.1; NZ_ACQT01000011.1.
DR AlphaFoldDB; C5T1G0; -.
DR PATRIC; fig|573060.9.peg.4487; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000003856; 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; 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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003856}.
FT DOMAIN 3..35
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 82..160
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 165..273
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 284..452
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 473..593
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 598 AA; 65096 MW; 97595E50D597DA8E CRC64;
MPTYTPPLRD MQFVMHEVLK VSDEFKALPP HAEVDADTIN AVLEEGGKFA AEVAFPLNIS
GDTEGCKLDK STHEVTTPQG FKEAYAKYVE GGWAALSCDP AYGGQGLPFV VNQCFYEMMN
SANQAWTMYP GLSHGAYECL HAHGTEEQKK IYLPKLTSGE WTGTMCLTEP HCGTDLGLLR
TKAEPQADGT YKITGAKIFI SAGEHDMTSN IVHLVLARLP DAPVGSKGIS LFVVPKFKVN
ADGSLGERNA IYCGGLEHKM GIHGNATAQI VIDGATGTMV GQPNKGLAAM FVMMNAARLG
VGNQSLGLTE VAYQNALAYA KDRIQMRSLS GTKAKDKPAD PIIVHPDVRK MLLTAKAYAE
GGRALQCFCA LLLDKELSHP DEKVRKESGE MLALLTPIVK AFITDNGYEA ATMCQQVFGG
HGYIKEWGME QYVRDARINM IYEGTNTIQS LDLLGRKILG NNGATLKKFG KLVGQLVEEE
GVNEKMAEFI NPIAYLGDQM TKFTTEIGFR GMQNPDEVGA AAVDYLRVAG HLVFGYFFAR
MAQVALREIA AGNTDPFYQA KLQTARFYFA KLFPETATLM RTARAGSKVL MDTDLALA
//
