(data stored in ACNUC7421 zone)

SWISSPROT: Q13DI9_RHOPS

ID   Q13DI9_RHOPS            Unreviewed;       388 AA.
AC   Q13DI9;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   16-JAN-2019, entry version 70.
DE   SubName: Full=Acyl-CoA dehydrogenase-like {ECO:0000313|EMBL:ABE37850.1};
GN   OrderedLocusNames=RPD_0612 {ECO:0000313|EMBL:ABE37850.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37850.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37850.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37850.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE37850.1; -; Genomic_DNA.
DR   RefSeq; WP_011501037.1; NC_007958.1.
DR   STRING; 316057.RPD_0612; -.
DR   EnsemblBacteria; ABE37850; ABE37850; RPD_0612.
DR   KEGG; rpd:RPD_0612; -.
DR   eggNOG; ENOG4105C1G; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000131659; -.
DR   KO; K00249; -.
DR   OMA; GFPHDFH; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; RPAL316057:RPD_RS03140-MONOMER; -.
DR   Proteomes; UP000001818; 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; Q13DI9.
DR   SWISS-2DPAGE; Q13DI9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN        6    118       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      123    220       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      233    379       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   388 AA;  42932 MW;  3D6A1909D14F26D3 CRC64;
     MDFALTDQQE AIRDAIARIC EGFDDAYWLR KDREGGFPHD FHKALADAGW LGICVPEDYG
     GSGLGITEAA IMMRTISESG AGMSGASAVH INVFGLNPVV VFGTEEQRKR MLPPMVEGRE
     KACFAVTEPN TGLNTTQLKT RAVRNGDRYI VNGQKVWIST AQVAHKILLL ARTTPLEEVK
     SPTHGLSLFY TDFDRTKIQV HEIEKMGRKI VDSNELFFED FEIPLEDRIG EEGRGFQYIL
     EGMNPERILI AAEAVGLGKL ASSRASEYAK TRIVFNRPIG QNQAIQHPLA KNWVELEAAW
     LMVMSAAWQY DKGMPCAAAA NAAKYLAGEA GFQACEQAVM THGGFGYAKE YHVERYLREV
     LIPRIAPVSP QLALSFIAEK VLGLAKSY
//

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