ID D1AEY3_THECD Unreviewed; 734 AA.
AC D1AEY3;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACY99527.1};
GN OrderedLocusNames=Tcur_3998 {ECO:0000313|EMBL:ACY99527.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99527.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY99527.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; CP001738; ACY99527.1; -; Genomic_DNA.
DR RefSeq; WP_012854311.1; NC_013510.1.
DR AlphaFoldDB; D1AEY3; -.
DR STRING; 471852.Tcur_3998; -.
DR KEGG; tcu:Tcur_3998; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_9_3_11; -.
DR OrthoDB; 3778631at2; -.
DR Proteomes; UP000001918; 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; 2.
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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43292:SF4; ACYL-COA DEHYDROGENASE FADE34; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 215..337
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 370..462
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 466..549
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 572..721
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 734 AA; 78817 MW; 356E40066ED0DF8E CRC64;
MAIGLTEEHE ALAASVRGLA ERHITAQVVR EAVESAEHPR RPRFWQALAD QGLLGLHLPE
EYGGQGFGLV EQAVALEELG RALAPGPYVP TVLAAAAIAA YASKEAKAAL LPGLADGSRT
AAVALRGDFT AAPGGDGGAR ISGATETVLC ATQADLLVLP LGEDRWAVVD AEAAQITALD
ALDLTRPVAR VEVSDVTVPA ERIFQGALGD LAVVVLGAEA CGVAGRAVEE AAGYAKIREQ
FGRPIGQFQG IKHKCARMLI AAERARAAVW DAARAIDAGE EPDQRGYAIA VAGALVADAA
VDCAEDNIQV HGGIGYTFEH DAHLYYRRAM TLRALIGRPS RYRERAARLA LAGVRRPMDI
ELPPEAEQLR ERVRAEVAEL AEMDPFTQRA AMAEGGWVTP HLPKPWGKDA GPVEQIVIQQ
ELKRAGVRPV PLMIAGWVVP SLVAYGTPEQ QQRFLPPTLR GEILWCQLFS EPGAGSDLAS
LTTRAEKVEG GWKLTGQKIW NSLAREAQWG ICLARTDPDA PKHEGITYFL VDMKSPGLEV
RPLRECTGEA VFNEVFLDGV FVPDELVVGP VNQGWKVARN TLANERVGLT GSFQLGASLR
KLVSLIGDLG LADDPVVRDN LGDLVADEHT YLLLGLRATL KQISGTDPGV TANVRKLVAM
EHGQRVTEYG FTLLGEDGML NGGRKAELRH RWSFYMLASR AMTIGGGTTE VNLNVIGERI
LGLPRDPEPV RDRS
//
