ID A0A1I1EVH2_9ACTN Unreviewed; 622 AA.
AC A0A1I1EVH2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SAMN04487968_102243 {ECO:0000313|EMBL:SFB90686.1};
OS Nocardioides terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=574651 {ECO:0000313|EMBL:SFB90686.1, ECO:0000313|Proteomes:UP000198832};
RN [1] {ECO:0000313|EMBL:SFB90686.1, ECO:0000313|Proteomes:UP000198832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7056 {ECO:0000313|EMBL:SFB90686.1,
RC ECO:0000313|Proteomes:UP000198832};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOLB01000002; SFB90686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1EVH2; -.
DR STRING; 574651.SAMN04487968_102243; -.
DR OrthoDB; 142556at2; -.
DR Proteomes; UP000198832; Unassembled WGS sequence.
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; 2.40.110.20; -; 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; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
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; 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:UP000198832}.
FT DOMAIN 3..34
FT /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT /evidence="ECO:0000259|Pfam:PF12418"
FT DOMAIN 162..276
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 296..462
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 481..618
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 622 AA; 67744 MW; D39AA09C34FB454D CRC64;
MSHYKSNLRD VEFNLFEVFG RDKILGTGAY ADLDVDTAKE ILAEIERISR EDLAPSMVES
DRTPPVFDPV TNTAPVPAAF KKSYDAWMES GFWSLQAPAE VGGTAAPQSL IWSSAEFILG
ANAPVWMYGC GPFFSRVVFE NGTDRDKRIA EIMVERLWGA TMVLTEPDAG SDVGAGKTFA
TANEDGSWNI SGVKRFITSA ESDLQENIMH LVLARPRGVE GVGGPGTKGL SLFLVPKYHF
DHRTGELTGE RNGVYVTNVE HKMGIKVSNT CELTFGDPQV GGGEPAQGWL LGEVHDGIRQ
MFDVIENARM MVGTKAIATL STGYLNALEY AKTRVQGADL TNNAKDAPRV TITHHPDVRR
SLLVQKSFAE AMRALVIYTA TWQDDVSIAK HNGETNQLAV DVNDLLLPIV KGYGSERSWT
ILGTESLQTL GGSGFLQEYP IEQYVRDAKI DTLYEGTTAI QGQDFFFRKI VKNQGVALGH
LAGEIKSFLA EEGHGELKES RALLTTALAD AEAIVSHMFT DLLSSDPSSA SGDIGNIYKV
AQNTSRLLMV LGDVICAWLL LRQAEVALER LGGDAGKDKS FYEGKVAAAK FFASYNLPKL
SAERAIAEAI DNSIMELDEA AF
//
