ID F6EMU6_HOYSD Unreviewed; 633 AA.
AC F6EMU6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AEF42838.1};
GN OrderedLocusNames=AS9A_4405 {ECO:0000313|EMBL:AEF42838.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF42838.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF42838.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002786; AEF42838.1; -; Genomic_DNA.
DR RefSeq; WP_013809186.1; NC_015564.1.
DR AlphaFoldDB; F6EMU6; -.
DR STRING; 443218.AS9A_4405; -.
DR KEGG; asd:AS9A_4405; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_034827_0_0_11; -.
DR OrthoDB; 5427839at2; -.
DR Proteomes; UP000009235; Chromosome.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF19; ACYL-COA DEHYDROGENASE FADE4-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT DOMAIN 263..406
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 633 AA; 70432 MW; 44E89C960AB1950C CRC64;
MTSASNNLFN PKSPDFSHFD AKTQELFGVT IGFFESRGKD WLKQQDRDRV WYSDFLDLVK
KERIFATFLT PSSEANGDPD KRWDTARNAM YSQILGFYGM QYWYVWQVTI LGLGPIWQSK
NAKARAKAAA LLEAGEIFAF GLSEQEHGAD VYSTDMVLDP QEETEGGYTA NGGKYYIGNG
NLAAMVSVFG RRSDKPIIDS ADIERHRPAE DFEGYVFFAA DSQHQNYKLR KNVVDAQMYV
AAFVLENYPV AADDILHAGK SAFHAAINTV NIGKFNLGFG AIGACEHAMF EALTHAENRI
LFGQRVTEFS QIRRMTAEAY ARLVGMKLYS ERAIDYMRSA APDDRRYLLF NAIEKMNVTR
EGEKIVTLLS DTIAARAFES DMYFTMALLG VTGLPRLEGT VHVNMALSLK FMQNYMFRAT
DAGLAALRVL PMGSAPRGVV RTLATGLRGA SSAFATLPRV RAELPAVPTR RDAANDDFLF
RQGPSAGLSK IQFTDWRPLL REFAHIPNVA VFLAQAEALQ TLLVAASPTP AQQKDVDFLF
TLGELFTLVP YAQLILEQAK IENTNGYILD HLFELLVTDF SGHATTLHCK TTATKAQKTR
ALDLVQQPAA DQLRFDKVVA DARSIAGGYE MGR
//
