ID A0A0S8B8J3_9PROT Unreviewed; 367 AA.
AC A0A0S8B8J3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KPK07904.1};
GN ORFNames=AMJ64_05225 {ECO:0000313|EMBL:KPK07904.1};
OS Betaproteobacteria bacterium SG8_39.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK07904.1, ECO:0000313|Proteomes:UP000051483};
RN [1] {ECO:0000313|EMBL:KPK07904.1, ECO:0000313|Proteomes:UP000051483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_39 {ECO:0000313|EMBL:KPK07904.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK07904.1}.
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DR EMBL; LJTQ01000033; KPK07904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8B8J3; -.
DR STRING; 1703390.AMJ64_05225; -.
DR PATRIC; fig|1703390.3.peg.1731; -.
DR Proteomes; UP000051483; 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; IPR013107; Acyl-CoA_DH_C.
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:SF41; ACYL-COA DEHYDROGENASE YDBM-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
FT DOMAIN 12..83
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 233..343
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 367 AA; 38980 MW; BEFF18AAFFC99981 CRC64;
MGVARELGTG FAKRAATVDE EDRFVGENYA DLKTSGLFAA AVPGELGGAG ASHAEMCSVV
RELARHCGST ALAFSMHTHQ VMTNAWRWRH AKAPVEALLK RIAAENIVLL SSGGSDWLQG
SGSATRVDGG FRIDARKIFT SGAPAGDLLL TSAVYEDPEA GPTVLHFGVP MTSDAVRIES
TWRVMGMRGT GSHDVTIDGF FLPDAAVGGT RPQGKWHPLF HVISMIAIPL IYSVYVGIAE
AARDRALAFA AKRRTDHHLL DLIGGMENAL AAARLALGEM IAAAQTNQPG AAVTSRVFIA
RTLAARAAIE AVEQAMLVAG GSAFYRGNGL ERLFRDVQAA RYHPLQEGLQ RELAARIALG
RNIDGGQ
//
