(data stored in SCRATCH zone)

SWISSPROT: B2UH98_RALPJ

ID   B2UH98_RALPJ            Unreviewed;       391 AA.
AC   B2UH98;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACD28949.1};
GN   OrderedLocusNames=Rpic_3835 {ECO:0000313|EMBL:ACD28949.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD28949.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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; CP001069; ACD28949.1; -; Genomic_DNA.
DR   RefSeq; WP_012429993.1; NC_010678.1.
DR   STRING; 402626.Rpic_3835; -.
DR   EnsemblBacteria; ACD28949; ACD28949; Rpic_3835.
DR   GeneID; 6284930; -.
DR   KEGG; rpi:Rpic_3835; -.
DR   PATRIC; fig|402626.5.peg.76; -.
DR   eggNOG; ENOG4105C1G; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000131659; -.
DR   KO; K00249; -.
DR   OMA; CPPSKAF; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; RPIC402626:GH94-3845-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
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; B2UH98.
DR   SWISS-2DPAGE; B2UH98.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN       14    125       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      129    222       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      234    382       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   391 AA;  42115 MW;  763711A334051C44 CRC64;
     MSDKDYLQWP FFDDKHRQLE AELDAWATKH IAHDHGPDVD AECRALVKLL GQGGWLRHAV
     GGTAHGGAGE TIDTRAICLI RETLARHSGL ADFAFAMQGL GSGAISLHGT PEQRERYLTK
     VAHGEAISAF ALSEPDAGSD VAAMASAARE DGNDYVLDGE KTWISNGGIA DFYVVFARTG
     EAPGSRGISA FIVEAGTPGF EIAERINVIA PHPLARLRFT NCRIPASQRV GAAGEGFKVA
     MRTLDVFRTS VAAAALGFAR RALDEALARA TTRKMFSGVL ADFQLTQAKL AQMATAIDSA
     ALLTYRAAWQ RDQGRNVTRE AAMAKLTATE NAQQVIDAAV QMWGGLGVVS EQPVERLYRE
     IRSLRIYEGA TEVQQLIIAR ELLRAAAPAK S
//

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