ID A0A1J5BZ56_9BURK Unreviewed; 598 AA.
AC A0A1J5BZ56;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OIP13226.1};
GN ORFNames=AUK50_14000 {ECO:0000313|EMBL:OIP13226.1};
OS Comamonadaceae bacterium CG2_30_57_122.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1805089 {ECO:0000313|EMBL:OIP13226.1, ECO:0000313|Proteomes:UP000182154};
RN [1] {ECO:0000313|EMBL:OIP13226.1, ECO:0000313|Proteomes:UP000182154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_57_122 {ECO:0000313|EMBL:OIP13226.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIP13226.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNXW01000315; OIP13226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5BZ56; -.
DR Proteomes; UP000182154; 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}.
FT DOMAIN 4..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..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 473..593
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 598 AA; 64780 MW; 7BF5B0C0EE4C5817 CRC64;
MAVYTPPLRD MQFVMHELLN VTADLAAMPA HADMDAETIN AVLEEGGKFA SEVLLPLNIS
GDTEGCKLDI TTHAVTTPAG YKQAYKQYIE GGWAALACDP EFGGQGLPLV VNQCFYEMMN
SANQAWTMYP GLTHGAYAAL HTHGTPEQKA TYLHKMTSGE WTGTMCLTEP HCGTDLGLMR
TKAEPQGDGT YKITGNKIFI SAGEHDLADN IIHLVLARLP DAPPGIKGVS LFIVPKFLVN
ADGSVGARNG IYCGGLEHKM GIKSNATAQI VLEDAVGTMV GQPNKGMQGM FVMMNAARLG
VGNQSLGLTE VAFQNALVYA KDRIQMRALT GPKAKDKPAD PIIVHPDVRK MLLTAKAYAE
GGRALLCFSS MLLEKEHNHP DEQVRKESGE LLALLTPICK AFLTDNGHIS TNACMQVFGG
HGFIKEWGME QFVRDNRINM IYEGTNTIQS LDLLGRKVLS NNGATLRKFG KLVGALVAEE
GVNEKMAEFI TPVAILADQM TKFTTEIGFK GFQNPDEVGA AAVDYLRVAG HLVYGYFWAR
MAQVALKQIA AGNADPFYVA KLQTARFYFA KLFPETATLM RTARAGSKVL MDTDAALA
//
