(data stored in SCRATCH zone)

SWISSPROT: C0ZN59_RHOE4

ID   C0ZN59_RHOE4            Unreviewed;       401 AA.
AC   C0ZN59;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 52.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAH31111.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:BAH31111.1};
GN   OrderedLocusNames=RER_04030 {ECO:0000313|EMBL:BAH31111.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31111.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31111.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH31111.1; -; Genomic_DNA.
DR   RefSeq; WP_020905915.1; NC_012490.1.
DR   STRING; 234621.RER_04030; -.
DR   EnsemblBacteria; BAH31111; BAH31111; RER_04030.
DR   GeneID; 31540261; -.
DR   KEGG; rer:RER_04030; -.
DR   PATRIC; fig|234621.6.peg.844; -.
DR   HOGENOM; HOG000131668; -.
DR   BioCyc; RERY234621:GHDE-412-MONOMER; -.
DR   Proteomes; UP000002204; 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; -; 1.
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.
PE   3: Inferred from homology;
DR   PRODOM; C0ZN59.
DR   SWISS-2DPAGE; C0ZN59.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW   ECO:0000313|EMBL:BAH31111.1}.
FT   DOMAIN        6    119       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      123    216       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      228    382       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   401 AA;  43289 MW;  FC3E6E6ABA90A96C CRC64;
     MYLDLSEESK TLRKELRAYF AEIINDEDRR ALVDQTEGGP VFDRILRRMG KDGWLGLGWP
     EEFGGRGENP EALYVFYDEV IRANAPLSLV TLNTVGPALI KHGTQAQKDF FLRPILAGEL
     IFAIGYTEPN AGTDLAALET RARIEGDELV INGNKIFTSA GVFADWVWLA VRTDPDAPTH
     QGISVVLVPT NSPGFSVTEI HTVGGISTSA TYYEDVRVPI SNVVGELNQG WKLITNQLNH
     ERVALAARGG IANELFAEVV EWAKTEPAGD GHVYDIGWVR EKLAEVYALL SAADLMNLRL
     VADVAANTLG GGDSAAAKIF GTEAVVSAYG MLQEVLGAKG LLRPGTPGAV LEGRVENLGR
     RAQNNTFGGG TNEVMREIVA AKCLGMALAA RRRPAAQNEK S
//

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