ID H8GTR1_DEIGI Unreviewed; 400 AA.
AC H8GTR1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:AFD25389.1};
GN OrderedLocusNames=DGo_CA1462 {ECO:0000313|EMBL:AFD25389.1};
OS Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD25389.1, ECO:0000313|Proteomes:UP000007575};
RN [1] {ECO:0000313|EMBL:AFD25389.1, ECO:0000313|Proteomes:UP000007575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC {ECO:0000313|Proteomes:UP000007575};
RX PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA Lin M.;
RT "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT Deinococcus gobiensis: insights into the extreme environmental
RT adaptations.";
RL PLoS ONE 7:E34458-E34458(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; CP002191; AFD25389.1; -; Genomic_DNA.
DR RefSeq; WP_014684872.1; NC_017790.1.
DR AlphaFoldDB; H8GTR1; -.
DR STRING; 745776.DGo_CA1462; -.
DR KEGG; dgo:DGo_CA1462; -.
DR PATRIC; fig|745776.4.peg.1504; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_0; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000007575; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 19..127
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 134..233
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 249..394
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 136..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43072 MW; 7CCE8639FE902BAD CRC64;
MTSTLTPPTN PNVTPQSGDQ RTILSALRGF LKDRVEPGAA ERDQTGEFPH DIVRGLGELG
IMGAQTPEIY GGSELDTATF AMIIEEIAAV DGSLCLTVAS HNSLCQGHIL IGGTEAQKRK
FLPDLASARK LGAWGLTEPG SGSDSGGMTS RAAEQPDGSW VLNGSKNFIT QGSVGGTYVV
LARTDPAREG RGKNDGISAF VFNRDEVQGF SIGRKEDKLG LRSSDTAQLI FEDIHLPAGA
LLGERGNAFK DVMRVLDGGR VGIAAMGLGL GRAAFEYAAR YTLGREQFGK PIAHNQNLAF
RLADLDTRLE AARLLIRKAA DLKDAGQNFT VPVARAKLFA TTVGVEACDE AIQMLGGYGY
IKEYPVERFW RDNRLTRIGE GTDEVQRLVI SRDVLRRFAD
//
