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Database: UniProt
Entry: A0A290XGD1_9GAMM
LinkDB: A0A290XGD1_9GAMM
Original site: A0A290XGD1_9GAMM 
ID   A0A290XGD1_9GAMM        Unreviewed;       596 AA.
AC   A0A290XGD1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ATD68190.1};
GN   ORFNames=CNR27_12720 {ECO:0000313|EMBL:ATD68190.1};
OS   Luteimonas chenhongjianii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Luteimonas.
OX   NCBI_TaxID=2006110 {ECO:0000313|EMBL:ATD68190.1, ECO:0000313|Proteomes:UP000218968};
RN   [1] {ECO:0000313|Proteomes:UP000218968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=100111 {ECO:0000313|Proteomes:UP000218968};
RA   Gui Z.;
RT   "Luteimonas liuhanmingii sp.nov., isolated from the intestinal contents of
RT   Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL   Submitted (SEP-2017) 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; CP023406; ATD68190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A290XGD1; -.
DR   KEGG; lum:CNR27_12720; -.
DR   OrthoDB; 9764895at2; -.
DR   Proteomes; UP000218968; Chromosome.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12418; AcylCoA_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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218968}.
FT   DOMAIN          3..33
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          81..158
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          164..273
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          284..452
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          468..589
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   596 AA;  64131 MW;  661AE38017440E26 CRC64;
     MSTYHAPLTD IRFALHDVLQ VEPLFASLGF EDAGRETLDA VLDECARLCE TVLAPLNRIG
     DEVGVSFDKA TGAVTTPTGF KDAYDQFVEG GWTGISAPVE FGGMGLPHGI GICLEEMIDA
     ANLAWSNFPL LSHGAVNALH HHGEDWQKDV FLKPLIAGTW TGTMCLTEPQ CGTDLGLLKT
     RAEPQADGSY AITGTKIFIT AGEHDLTDNI IHLVLARLPD APEGSRGISL FIVPKMQVGR
     DGSVGTRNAV RCGAVEHKMG IHGSATCVMN FDGAQGYLIG HPHKGLMAMF TMMNTARLGV
     GIQGLGLATR AYENALRYAR ERLQSRALSG AKLPSKPADP ILVQPDVRRM LLTCKALTEG
     GRLLAYHAGS LVDSAAHAQD PLARKQADDL LGFLTPIVKG CLTEWGNECT YHALQCYGGH
     GYIAEHGMEQ LARDARITTL YEGTTGIQAL DLMGRKTMQL QGAGLRVFLG MIETFCTTHA
     EDVALAEFVV PLRAKAAEWQ QLTRSIAERA AADPEEIGAA AHDYLFFSGY VALAYWWARS
     VAVAEASARP ETFKAGKRET ARFYFTRILP RTLGHAAAIA SGPASLLSIP DDALDS
//
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