ID C5DAV2_GEOSW Unreviewed; 387 AA.
AC C5DAV2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Acyl-CoA dehydrogenase type 2 domain protein {ECO:0000313|EMBL:ACS24416.1};
GN OrderedLocusNames=GWCH70_1626 {ECO:0000313|EMBL:ACS24416.1};
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS24416.1};
RN [1] {ECO:0000313|EMBL:ACS24416.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS24416.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001638; ACS24416.1; -; Genomic_DNA.
DR AlphaFoldDB; C5DAV2; -.
DR STRING; 471223.GWCH70_1626; -.
DR KEGG; gwc:GWCH70_1626; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_3_2_9; -.
DR OrthoDB; 9785203at2; -.
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:SF41; 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; 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;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 11..100
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 249..367
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 130..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 43736 MW; 7603BAD6B38E25CA CRC64;
MNELYHLFLR TERERNLYER ARNLAERFQK RARWHDEHAE FPFENFDDLK EARFLSLTVP
KSYGGEEISL YEFLLIQETI AQGDGATALS LGWHLGIIMN LAETKKWPLS VFERICREVV
EKQILLNSAH SEEATGSPAR GGKPETTAEH RSGRWVISGR KTFTSLAPAL DYFIVSATIQ
ETGEVGNFLI PKTAAGLKIE KTWDTLGMRA TRSDDVILEN VEVEEEALVE MLSLPKAKSH
AQGWLLHIPA CYLGIAIAAR NEAIAFAKTY QPNSLSHPIA EVPEVRRKIA QMDIHLMAAR
HFMYSIADQW DRYPEKRAQM KEELAAVKYI ATNTAVDVVD LAMRIVGGKS LFAENPLQRH
YRDVRAGLHN PPADDITVSI VSGRALQ
//
