(data stored in SCRATCH zone)

SWISSPROT: C4KEH2_SULIK

ID   C4KEH2_SULIK            Unreviewed;       546 AA.
AC   C4KEH2;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 42.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACR41169.1};
GN   OrderedLocusNames=M164_0541 {ECO:0000313|EMBL:ACR41169.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR41169.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR41169.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001402; ACR41169.1; -; Genomic_DNA.
DR   RefSeq; WP_009071332.1; NC_012726.1.
DR   ProteinModelPortal; C4KEH2; -.
DR   EnsemblBacteria; ACR41169; ACR41169; M164_0541.
DR   GeneID; 7809989; -.
DR   KEGG; sid:M164_0541; -.
DR   HOGENOM; HOG000253935; -.
DR   OMA; YGDKWFC; -.
DR   OrthoDB; POG093Z06CE; -.
DR   BioCyc; SISL426118:GI01-553-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
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   CDD; cd01154; AidB; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   InterPro; IPR034184; AidB.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KEH2.
DR   SWISS-2DPAGE; C4KEH2.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   FAD {ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT   DOMAIN      162    261       Acyl-CoA_dh_M. {ECO:0000259|Pfam:
FT                                PF02770}.
FT   DOMAIN      274    432       Acyl-CoA_dh_1. {ECO:0000259|Pfam:
FT                                PF00441}.
FT   COILED      435    462       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   546 AA;  62399 MW;  75048B1764E9A537 CRC64;
     MSKGNSPFSY ISSAYGKNHF NIDKPLQKIL EYFDVKADFS KLGEFAGGEL YEIAEHVDKR
     ARPIHVMWSV NGERVDEVWI DPSLRAAIKR LIKDFDINKF PYKEENWHKH YASIYLVSDP
     GIACILTITN QTAYALYKYG SEELKKYVPY LIGDSDELLF GATWFTEIQG GSDLGSNLVE
     AEFNGKYWLL KGNTKYFASG VGLADLALVS ARPMGSKSGA KGLSLFLVPK KNNKGEKNFL
     IRRLKRKSGT NSVPTGEVEF NSSEAYLIGE KEYGIYYITE DLMVSRLSNA VGALGIARKS
     FLESYYYSQS RKAFGKALIE HPLIQKDLLE MELMIEGGMV VTFKAIDQFQ KSWKAMPPFY
     NEQYHYARLL THISKHITAE IASQVSRMAM EIHGGIGFLE EFPIERLHRE ALITPIWEGT
     GNIQALEMLE AMVKKEAHRQ LIRDLEGIVN EAKDEIASKT LDFIKDKATT LLTYREYEMQ
     FYSKDLLLTL GHGISVILLS HMGRKLGIER FTMLSKIYYE RFLMGRSILR DYISEIRELI
     NMEEMK
//

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