(data stored in ACNUC7421 zone)

SWISSPROT: A8FQC3_SHESH

ID   A8FQC3_SHESH            Unreviewed;       475 AA.
AC   A8FQC3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 73.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   OrderedLocusNames=Ssed_0433 {ECO:0000313|EMBL:ABV35046.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35046.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35046.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35046.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC       {ECO:0000256|RuleBase:RU003692}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692};
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000256|RuleBase:RU003692}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003692}.
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DR   EMBL; CP000821; ABV35046.1; -; Genomic_DNA.
DR   RefSeq; WP_012140783.1; NC_009831.1.
DR   ProteinModelPortal; A8FQC3; -.
DR   STRING; 425104.Ssed_0433; -.
DR   EnsemblBacteria; ABV35046; ABV35046; Ssed_0433.
DR   KEGG; sse:Ssed_0433; -.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; TMSEAVM; -.
DR   OrthoDB; POG091H0239; -.
DR   BioCyc; SSED425104:GH7Q-455-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQC3.
DR   SWISS-2DPAGE; A8FQC3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   FAD {ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692}.
FT   DOMAIN        8    328       FAD/NAD-binding_dom. {ECO:0000259|Pfam:
FT                                PF07992}.
FT   DOMAIN      347    455       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
SQ   SEQUENCE   475 AA;  50799 MW;  9748FFD1FC841065 CRC64;
     MSNEIKTQVL VVGAGPAGYS AAFRAADLGL EVIIVERFNT LGGVCLNVGC IPSKALLHVS
     KVIEEAKAVA SHGVVFGEPQ IDLDKLRSFK ETVISQLTTG LGGMSKMRKV DVVNGFGKFT
     SPNTIEVTGE DGVKVIRFEQ AIIAAGSRPI QLPFIPHEDP RIWDSTDALE LKEVPGKLLV
     MGGGIIGLEM GTVYSSLGSE IDVVEMFDQV IPAADKDIVR VYTKKIKKKF NLILQTKVTA
     VEAKEDGIYV SMEGKKAPAE PVRYDAVLVA IGRTPNGKLI DAEKAGVNID ERGFINVDKQ
     MRTNVPNIYA IGDIVGQPML AHKGVHEGHV AAEVISGLKH FFDPKVIPSI AYTDPEVAWV
     GLTEKEAKEQ GVAYETATFP WAASGRAIAS DCSDGMTKLI FDKETHRVIG GAIVGVNGGE
     LLGEIGLAIE MGCDAEDLAL TIHAHPTLHE SVGLAAEIYE GSITDLPNPK AKKKK
//

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