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Database: UniProt
Entry: L1KUR9_9ACTN
LinkDB: L1KUR9_9ACTN
Original site: L1KUR9_9ACTN 
ID   L1KUR9_9ACTN            Unreviewed;       390 AA.
AC   L1KUR9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Acyl-CoA dehydrogenase, C-terminal domain protein {ECO:0000313|EMBL:EKX64367.1};
GN   ORFNames=STRIP9103_03590 {ECO:0000313|EMBL:EKX64367.1};
OS   Streptomyces ipomoeae 91-03.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX64367.1, ECO:0000313|Proteomes:UP000010411};
RN   [1] {ECO:0000313|EMBL:EKX64367.1, ECO:0000313|Proteomes:UP000010411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-03 {ECO:0000313|EMBL:EKX64367.1,
RC   ECO:0000313|Proteomes:UP000010411};
RA   Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKX64367.1}.
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DR   EMBL; AEJC01000376; EKX64367.1; -; Genomic_DNA.
DR   RefSeq; WP_009321194.1; NZ_AEJC01000376.1.
DR   AlphaFoldDB; L1KUR9; -.
DR   PATRIC; fig|698759.3.peg.4983; -.
DR   OrthoDB; 3404950at2; -.
DR   Proteomes; UP000010411; Unassembled WGS sequence.
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; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR48083:SF5; NRGC PROTEIN; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000010411}.
FT   DOMAIN          18..98
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          242..364
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   390 AA;  42505 MW;  F072EF893AD9A37F CRC64;
     MTNTQAVPNT AAEILAAAKA LAPQLRERAV EIEQNRRLPA DVVELIRATG AFRMGFSKAW
     GGPELTSIEQ TEVVEALAYG DSGAGWAAMI GMDSGLYASF LDETVAKEMF PRLDMATAGL
     LFPTGRAERV DGGYRLTGRW QFGSGITHAD WVISGAFIYE DGEPFLVDGS HDSILLMVPQ
     EDVEIIDTWH TTGLAGSGSC DYAIHDVFVP EERTLTFGAV RNGEGPLAQP EVHMRNMPGV
     PLGVARAALD WVRAKVVAKP GWSDNWRVQV TLAECEADFN ATRSAVYGAM RRQWDVLEAG
     GTLDDLTADE RAALPLSRLH AFRTVRSIVM RLYDVMQTAA IYKPSPLDRW LRDTMTMCQH
     VVAQDKILQS AGAHLLGSRP SFPLSLGITG
//
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