ID A0A1B1Z314_9BACI Unreviewed; 386 AA.
AC A0A1B1Z314;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ANX11790.1};
GN ORFNames=ABE41_007195 {ECO:0000313|EMBL:ANX11790.1};
OS Fictibacillus arsenicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX11790.1, ECO:0000313|Proteomes:UP000077412};
RN [1] {ECO:0000313|EMBL:ANX11790.1, ECO:0000313|Proteomes:UP000077412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-54 {ECO:0000313|EMBL:ANX11790.1,
RC ECO:0000313|Proteomes:UP000077412};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT toxicity to nematodes and a potential arsenic-resistance activity.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP016761; ANX11790.1; -; Genomic_DNA.
DR RefSeq; WP_066288143.1; NZ_CP016761.1.
DR AlphaFoldDB; A0A1B1Z314; -.
DR STRING; 255247.ABE41_007195; -.
DR KEGG; far:ABE41_007195; -.
DR Proteomes; UP000077412; Chromosome.
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 CDD; cd00567; ACAD; 1.
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; IPR013107; Acyl-CoA_DH_C.
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; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF25; ACYL-COA DEHYDROGENASE YDBM-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000077412}.
FT DOMAIN 23..98
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 129..221
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 247..365
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 386 AA; 42849 MW; 465196BE23C83B02 CRC64;
MSYLYDAYIK NETQQKWFSK IDILASKFAE RADKHDREGS FPFENVDELK KAGYLSLTIP
KEFGGEGLSL YEFVLLQERI AAGDAATALC LGWHLGCFLE LSEERSWKEE TFRSLCEKVV
NNQVLVNRAA SEPATGSPTR GGMPQTKAVK RGDDWVINGT KTFTSMAPAL DHAIVSAQIG
DTGKKGNFLI DMKQDGVTIE ETWDTVAMRG TRSDDLVMKD VKVNDESLVE EERGKLDFPK
AWLLHIPACY LGVAVAGRNE AVNFAKSYKP NSLPGAIAEV PEVQRKIGEM ELELFKAREL
LYSTAAKWVN EPESRMEMGP SLMAVKHVAT NSAAKVVDLA MRIVGARSLA MSSPLQRHYR
DVRAGLHNPP MDDMVISSLA KRALNE
//