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Database: UniProt
Entry: A0A344LH77_9PSEU
LinkDB: A0A344LH77_9PSEU
Original site: A0A344LH77_9PSEU 
ID   A0A344LH77_9PSEU        Unreviewed;       403 AA.
AC   A0A344LH77;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AXB47401.1};
GN   ORFNames=A4R43_37205 {ECO:0000313|EMBL:AXB47401.1};
OS   Amycolatopsis albispora.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB47401.1, ECO:0000313|Proteomes:UP000250434};
RN   [1] {ECO:0000313|EMBL:AXB47401.1, ECO:0000313|Proteomes:UP000250434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:AXB47401.1,
RC   ECO:0000313|Proteomes:UP000250434};
RA   Wang H., Chen S., Wu Q.;
RT   "Complete genome sequence and analysis of deep-sea sediment isolate,
RT   Amycolatopsis sp. WP1.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP015163; AXB47401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344LH77; -.
DR   KEGG; aab:A4R43_37205; -.
DR   OrthoDB; 3402961at2; -.
DR   Proteomes; UP000250434; 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   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          28..93
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          252..384
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   403 AA;  44082 MW;  9D6B9370A3544A83 CRC64;
     MTATVEIPEP ELTPDQVVAR AEAIAPTLVE RQAETEKRGY YAEDTHEAFR AAGFYRILVP
     RRYGGYEFGL DTFMRVVQAL TRGCPSTGWM YCLGAAHAHA AASIFDERVQ DEIFAVGDFI
     CPATVAPGGE AEQLENGDWR LSGTWNYCSG SPYATHFIGH TLVFGEDGTP SPMMFVVPRE
     QWTRLDDWNT TLGLRGSGSH SILMENAHIP AHHMFEMHLS QVDVSGGTPG AALHQNPFYG
     GGLLSFMVLE DAVLAVGMAQ SALDACEELM KTRSTIFPPI QGRAQDPDYQ FRFGQATGMI
     ATAEAAFHNA IQQWERAAAE GSAAFTPERE LRIALICREV VRLSFDAVQA HLVPTAGSSA
     VRNGARVERV WRDLSMQHSH AGISVFLSAI AQREYSQARL GAA
//
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