(data stored in SCRATCH zone)

SWISSPROT: D4YX97_SPHJU

ID   D4YX97_SPHJU            Unreviewed;       599 AA.
AC   D4YX97;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   16-JAN-2019, entry version 46.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:BAI94979.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:BAI94979.1};
GN   Name=bcd {ECO:0000313|EMBL:BAI94979.1};
GN   OrderedLocusNames=SJA_C1-01450 {ECO:0000313|EMBL:BAI94979.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94979.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94979.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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; AP010803; BAI94979.1; -; Genomic_DNA.
DR   RefSeq; WP_013038797.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-01450; -.
DR   EnsemblBacteria; BAI94979; BAI94979; SJA_C1-01450.
DR   GeneID; 29271853; -.
DR   KEGG; sjp:SJA_C1-01450; -.
DR   eggNOG; ENOG4105CSU; Bacteria.
DR   eggNOG; COG1960; LUCA.
DR   HOGENOM; HOG000258862; -.
DR   KO; K00248; -.
DR   OMA; CMFHMMN; -.
DR   Proteomes; UP000007753; Chromosome 1.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
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; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12418; AcylCoA_DH_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YX97.
DR   SWISS-2DPAGE; D4YX97.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW   ECO:0000313|EMBL:BAI94979.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        9     37       AcylCoA_DH_N. {ECO:0000259|Pfam:PF12418}.
FT   DOMAIN       56    159       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      165    272       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      293    458       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
FT   DOMAIN      487    595       Acyl-CoA_dh_C. {ECO:0000259|Pfam:
FT                                PF12806}.
SQ   SEQUENCE   599 AA;  66373 MW;  5BF656C57D6833C0 CRC64;
     MTTLNSKLLS RTNLDFLLYD WLEAEAMTGR ERFADHDRAT FSTMIDTAEK IATDWFANHN
     AKGDKHEPYM EDGKVVLIPE IAKAYGAFRD AGFLATTNDA QYGGLQLPFV IDRACIAYFL
     AANIATSGYA FLTCAAANLL LAHGTPEQID RFALPMLAGR FTGTMCMSEP QAGSSLGDIR
     TRAELQPDGS YRLFGTKMWI SGGDHELSET IVHLVLARTG PAEHGVRGLS LFIVPKHIVR
     DGNPAERNDV ALVGLNHKMG NRATTNCVLS LGDGQFAVDG QAGAVGYRIG EENRGLSYMF
     HMMNEARIVV GLGAVMLGYT GYLHAVQYAR DRPQGRALTQ KGGDPVAIIQ HADVRQMLLT
     QKAYVEGGLA LCLYLAKLLD DQSTGDEETA RRAYLLLDLL TPIGKSWPAK WCLEANNLAI
     QVHGGAGYTH DFPVEQFYRD NRINAIHEGT HGIQALDLLG RKVLNGEAIA YLDSVIDDRC
     TSAAGSANPD TQEWARRLRS AWQDIQRVTE GLSREQDVER RLANAGLYLD AFGHVIIAWI
     WLEQVDALDR ATDVSEDFIL GKRQAARYFF DWELPKINHW LAILERLDST ALEMQDSWF
//

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