ID Q1J3V1_DEIGD Unreviewed; 412 AA.
AC Q1J3V1;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Acyl-CoA dehydrogenase-like protein {ECO:0000313|EMBL:ABF43833.1};
GN OrderedLocusNames=Dgeo_2399 {ECO:0000313|EMBL:ABF43833.1};
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OG Plasmid pDGEO01 {ECO:0000313|EMBL:ABF43833.1,
OG ECO:0000313|Proteomes:UP000002431}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF43833.1, ECO:0000313|Proteomes:UP000002431};
RN [1] {ECO:0000313|Proteomes:UP000002431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a {ECO:0000313|Proteomes:UP000002431};
RC PLASMID=pDGEO01 {ECO:0000313|Proteomes:UP000002431};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of plasmid 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000358; ABF43833.1; -; Genomic_DNA.
DR RefSeq; WP_011525657.1; NC_008010.2.
DR AlphaFoldDB; Q1J3V1; -.
DR KEGG; dge:Dgeo_2399; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_1_2_0; -.
DR Proteomes; UP000002431; Plasmid pDGEO01.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; 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; PTHR48083:SF13; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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|RuleBase:RU362125};
KW Plasmid {ECO:0000313|EMBL:ABF43833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002431}.
FT DOMAIN 10..134
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 138..239
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 251..400
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 412 AA; 46043 MW; A4E9C4A779D4232C CRC64;
MTLFDVSPRT QDLHARLSRF MDEYIYPNEA EFHRQVNEGN RWEHVQLIEE LKPRARAEGL
WNLFLPPASD PQGRFGPGLT NLEYAPLCEM MGRVWWAPEV FNCSAPDTGN MEVLARYGTP
EQQQQWLVPL LNGEIRSAFS MTEPEVASSD ATNIQARIRR DGDEYVINGR KWWTSGAGDP
RCRVSIFMGK TDPGAERHLQ QSMILVPLDT PGVRVERMLT VFGYDDAPHG HAEMTFENVR
VPAANLLLGE GRGFEIAQGR LGPGRIHHCM RLIGQAERAL ELMVERASRR VAFGKPLAAH
QHVREAIAHS RMEIDQARLL TLQAAHMMDT VGNKAARGQI AAIKVVAPNV ALRVIDRAIQ
VFGGAGVSQD TPLAMVYAQA RTLRLADGPD IVHIETVAKE ELRRQGVDGR GR
//
