(data stored in ACNUC7421 zone)

SWISSPROT: D4YXZ1_SPHJU

ID   D4YXZ1_SPHJU            Unreviewed;       412 AA.
AC   D4YXZ1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 39.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAI95223.1};
DE            EC=1.3.8.- {ECO:0000313|EMBL:BAI95223.1};
GN   OrderedLocusNames=SJA_C1-03890 {ECO:0000313|EMBL:BAI95223.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95223.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95223.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {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; BAI95223.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4YXZ1; -.
DR   STRING; 452662.SJA_C1-03890; -.
DR   EnsemblBacteria; BAI95223; BAI95223; SJA_C1-03890.
DR   KEGG; sjp:SJA_C1-03890; -.
DR   eggNOG; ENOG4105C9H; Bacteria.
DR   eggNOG; ENOG410XNTS; LUCA.
DR   HOGENOM; HOG000131660; -.
DR   KO; K00249; -.
DR   OMA; YINDYPM; -.
DR   OrthoDB; POG091H00BG; -.
DR   BioCyc; SJAP452662:GHEL-400-MONOMER; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
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; D4YXZ1.
DR   SWISS-2DPAGE; D4YXZ1.
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:BAI95223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        8    134       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      139    234       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      254    401       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   412 AA;  46186 MW;  A2489B8C4AC18D2B CRC64;
     MDFEQSAKSR EWMERVRAFM EEHIVPAVPV YHQQSAAIDR WTEIPPVFDE LKDKARQAGL
     WNIFMPPSEH DDEFFTSVGL TNVEYAPIAE LMGRISFASE VFNCMAPDTG NFEVLHRYGT
     AEQKQRFMVP LRDGKTRSAF LMTEPAVASS DARNIQTDIR RDGGDYVING RKWWSSGAGH
     PRCDFFIVMG KTDPDAAPYR QQSMILVPRD TPGVTLVRHL PVFGYDHAPH GHFEVALENV
     RVPAENMLLG EGCGFEIAQG RLGPGRIHHT MRNIATMEVA LEKMCRRLLS RRAFGKAIAE
     HSVWEERIAR ARCEIEMARL LCLKAAHMMD TVGNKAARAE IAMIKIAAPK MAQQIVDDAI
     QAHGGGGVSD DFGLAELWAN TRIVRLTDGP DEVHERQLAR MELAKYAEGA AS
//

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