(data stored in SCRATCH zone)

SWISSPROT: D4YXZ8_SPHJU

ID   D4YXZ8_SPHJU            Unreviewed;       392 AA.
AC   D4YXZ8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   16-JAN-2019, entry version 42.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAI95230.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:BAI95230.1};
GN   OrderedLocusNames=SJA_C1-03960 {ECO:0000313|EMBL:BAI95230.1};
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:BAI95230.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95230.1, 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; BAI95230.1; -; Genomic_DNA.
DR   RefSeq; WP_013039012.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-03960; -.
DR   EnsemblBacteria; BAI95230; BAI95230; SJA_C1-03960.
DR   GeneID; 29272083; -.
DR   KEGG; sjp:SJA_C1-03960; -.
DR   eggNOG; ENOG4105CC9; Bacteria.
DR   eggNOG; ENOG410XNVZ; LUCA.
DR   HOGENOM; HOG000131668; -.
DR   OMA; GELERGY; -.
DR   BioCyc; SJAP452662:GHEL-407-MONOMER; -.
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; 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; D4YXZ8.
DR   SWISS-2DPAGE; D4YXZ8.
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:BAI95230.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        6    122       Acyl-CoA_dh_N. {ECO:0000259|Pfam:
FT                                PF02771}.
FT   DOMAIN      128    218       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      274    389       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
SQ   SEQUENCE   392 AA;  42573 MW;  EEB0100084290B52 CRC64;
     MDLALTPEQR AFREEVRAFL AASLSPELRR GAALTSGVFA EPDIAREWQA ILEAKGWLVY
     HWPDHAGGPG WTPVQRWIFE KECAEAGAPI LPGMGLKLVG PVLYTYGTPA QKDHYLPRLR
     TAEHIWAQGF SEPGSGSDLA SLRTRAVRDG DHYVVSGHKI WTTQAHHANR LFALVRTDPH
     VKPQQGISFL LIDMALPGVT VKPILSASGD HELNEVFLDE VRVPVSDRVG EEGQGWSIAK
     FLLENERGGS SFAPAILADL ARLRTSTGPL TGELADRAVR LQLEAEALEM TELRTLIEIE
     HGAAPDPRSL TTKLLASEIR QGVEALAVDA FGLAGLQLPV ERPFYGDAMP TPIGSPEAQV
     AAARYLNARA WSIFGGTSEI QLTLIAKAAL GL
//

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