ID G2NMB2_STREK Unreviewed; 648 AA.
AC G2NMB2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:AEN12690.1};
GN ORFNames=SACTE_4864 {ECO:0000313|EMBL:AEN12690.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12690.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN12690.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN12690.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
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; CP002993; AEN12690.1; -; Genomic_DNA.
DR RefSeq; WP_014048641.1; NC_015953.1.
DR AlphaFoldDB; G2NMB2; -.
DR STRING; 862751.SACTE_4864; -.
DR KEGG; ssx:SACTE_4864; -.
DR PATRIC; fig|862751.12.peg.5042; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_11_1_11; -.
DR OrthoDB; 8876745at2; -.
DR Proteomes; UP000001397; 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; 2.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_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|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397}.
FT DOMAIN 64..169
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 174..270
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..440
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 70603 MW; 6DA2BAB179E04348 CRC64;
MSAPSDTPQA PKVTEREARQ VAEAAREQDW RKPSFAKELF LGRFRLDLLH PHPVPGAEDV
RRGEAFLDRL RAFCETHVDG ALIEREAKIP DDVVNGLKEL GALGMKIETR YGGLGLTQVY
YNRALALAGS ASPAIGALLS AHQSIGVPQP LKMFGTQEQK DTFLPRLART DISAFLLTEP
DVGSDPARLA TAAVPEGDDY VLDGVKLWTT NGVVADLLVV MARVPASDGH KGGITAFVVE
ADSPGITVEH RNAFMGLRGI ENGVTRFHGV RVPAANRIGP EGAGLKIALT TLNTGRLSLP
AMCVGVGKWS LKIAREWSAV REQWGRPVAR HEAVGAKISF IAATTFALEA VVDLSSQMAD
ESRNDIRIEA ALAKLYGSEM GWRISDELVQ IRGGRGFETA DSLAARGERA VPAEQMLRDM
RINRIFEGST EIMHLLIARE AVDAHLKVAG DIIDPDKPLS DKARAGVDAA GFYARWLPKL
VSGPGQLPNA YGEFRVPGHP DLSGHLRHVE RSARKLARST FYAMSRWQGR METKQNFLGR
IVDIGAELFA MSAACVRAEH LRATGDHGRE AYQLADVFCR QARLRVEELF ARLWANTDDI
DRRVVDGVLS GTYAWLEEGV IDPSGDGPWI ADATPGPATG ENVHRPIR
//
