ID A0A3E1R9B7_9BURK Unreviewed; 598 AA.
AC A0A3E1R9B7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RFO95927.1};
GN ORFNames=DIC66_15990 {ECO:0000313|EMBL:RFO95927.1};
OS Rhodoferax lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2184758 {ECO:0000313|EMBL:RFO95927.1, ECO:0000313|Proteomes:UP000260665};
RN [1] {ECO:0000313|EMBL:RFO95927.1, ECO:0000313|Proteomes:UP000260665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26218 {ECO:0000313|EMBL:RFO95927.1,
RC ECO:0000313|Proteomes:UP000260665};
RA Park M.;
RT "Rhodoferax soyangensis sp.nov., isolated from an oligotrophic freshwater
RT lake.";
RL Submitted (MAY-2018) 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:RFO95927.1}.
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DR EMBL; QFZK01000011; RFO95927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1R9B7; -.
DR OrthoDB; 9764895at2; -.
DR Proteomes; UP000260665; 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:UP000260665}.
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 164..274
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 472..593
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 598 AA; 65290 MW; 200B96E7AC7E240D CRC64;
MPTYTPPLRD MQFVMHELLH VMDDLQQIPK HAELDADTVN AVMEEGGKFA SEVLQPLNLS
GDMEGCRRDA ASHAVTTPKG FKEAYRQYID GGWAALACDP DFGGQGLPLV LNQMFYEMLN
SANQAWTMYP GLTHGAYAAL REHGTDAQKQ TYLHKMTSGE WTGSMCLTEP HCGTDLGLMR
TKAEAQGDGT YKITGTKIFI SAGEHDMADN IIHLVLARLS DAPPGIKGVS LFIVPKFHVK
SDGSLGARNG IFCAGLEEKM GIHGNSTCQM VLDGAVGTLV GQPNKGMQGM FVMMNAARLG
VGNQSLGLTE VAYQNALAYA KDRIQMRALT GPKSKDQAAD PIIVHPDVRK MLLTAKAYAE
GGRALMTFCS MLLEKEHYHP DEKVRKDSGE MLALLTPIVK AFITDNGWTA TSGCLQVFGG
HGYIKQTGME QLVRDARINM IYEGTNTIQS LDLLGRKVLS NNGATLRKFG KLIGQLVEEE
GVNEKMAEFI TPIAILGDQM TKFTTEIGFK AFQNPDEVGA AAVDYLRVAG HMVFGYFWAR
MAQVALKEIA SGNTDTFYVA KLQTARFYFA KLFPETATAM RTARSGARVL MDTDAVFA
//
