(data stored in ACNUC7421 zone)

SWISSPROT: Q47TV8_THEFY

ID   Q47TV8_THEFY            Unreviewed;       391 AA.
AC   Q47TV8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:AAZ54106.1};
GN   OrderedLocusNames=Tfu_0068 {ECO:0000313|EMBL:AAZ54106.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54106.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP000088; AAZ54106.1; -; Genomic_DNA.
DR   RefSeq; WP_011290515.1; NC_007333.1.
DR   STRING; 269800.Tfu_0068; -.
DR   EnsemblBacteria; AAZ54106; AAZ54106; Tfu_0068.
DR   KEGG; tfu:Tfu_0068; -.
DR   eggNOG; ENOG4105C1G; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000131659; -.
DR   OMA; MCDVHNT; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; TFUS269800:G1G4Q-68-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
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.
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; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TV8.
DR   SWISS-2DPAGE; Q47TV8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434}.
FT   DOMAIN       10    120       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      124    218       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      230    378       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   391 AA;  42218 MW;  5FE0361C6DA49AF2 CRC64;
     MSVTRLMPSQ ETADLVELVR EVASRELAPH VAEAEETERF PREAFRTLGK LGVLGLPYPE
     EYGGGGQPYE AYLNILEEIG AVWASVGVGV SVHVLSCYAL AVYGTEAQRQ RWLPDLLSGD
     LLGAYCLSEP HAGSDPAAMT TRARRDGDHY ILDGVKAWIT HGGQADFYTV MARTSDDRSR
     GISCFLVPAD TPGLSADRPE RKMGLTASHT TMLRFDGVRI PADQRIGAEG QGLSIALSSL
     DAGRLGIAAV ATGLAQAALD TAVDYARQRE AFGKPIIEHQ GLAFLLADMA AAVETARAAT
     LRAARLKDSG LPYSKEASIA KLIATDNAMR VTTDAVQVLG GYGYTRDFPV ERYMREAKVM
     QIFEGTNQIQ RLVIGRHLAR DATAHTVTVV R
//

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