ID B1M2F4_METRJ Unreviewed; 418 AA.
AC B1M2F4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Acyl-CoA dehydrogenase type 2 domain protein {ECO:0000313|EMBL:ACB26194.1};
GN OrderedLocusNames=Mrad2831_4227 {ECO:0000313|EMBL:ACB26194.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB26194.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB26194.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001001; ACB26194.1; -; Genomic_DNA.
DR RefSeq; WP_012321148.1; NC_010505.1.
DR AlphaFoldDB; B1M2F4; -.
DR STRING; 426355.Mrad2831_4227; -.
DR KEGG; mrd:Mrad2831_4227; -.
DR PATRIC; fig|426355.14.peg.4304; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_10_0_5; -.
DR Proteomes; UP000006589; 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 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 InterPro; IPR023922; S04_starv_induced_SfnB.
DR NCBIfam; TIGR04022; sulfur_SfnB; 1.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-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 40..140
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 260..393
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 43620 MW; 80A044BB832C5478 CRC64;
MSLNVDESAA DGAAEPLTPP LPPPPSPPHR IRSDAEALAA ARAVARVFAA GAAERDRDRR
LPWAEIAAFT ESGLGGITVP RAHGGAGVSH ATLAEVFAIL AAADGSAAQI PQNQFGVLAL
VAAAASPAQQ ARIYRDVLAG HRIGNAGPAR NGKAITNVDT RLTAGPEGPR LSGTRFYSTG
ALFAHWIPTR AVGPDGGPLL VFVRRDAPGV RVADDWQGFG QRTTASGTVV FAQAPVEADL
TIDLAPLAGR PGLFGPVSQL IHAAIDAGLA RGAAAAALDF LRSRTRPYPF TAETVAEDPH
ILGEIGRLTV DLHAAEEVLA RAGRALDRIA AAPVTAQSAA EASVAVAQAK ILTTEAALEA
SERLLELAGA SATRDGYNLG RYWRDARVHT LHDPVRWKYH LLGNHALNGV LPARHQWN
//
