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Database: UniProt
Entry: A0A1E3W562_9RHIZ
LinkDB: A0A1E3W562_9RHIZ
Original site: A0A1E3W562_9RHIZ 
ID   A0A1E3W562_9RHIZ        Unreviewed;       469 AA.
AC   A0A1E3W562;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   03-JUL-2019, entry version 17.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   ORFNames=AUC68_13470 {ECO:0000313|EMBL:ODS00931.1};
OS   Methyloceanibacter methanicus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methyloceanibacter.
OX   NCBI_TaxID=1774968 {ECO:0000313|EMBL:ODS00931.1, ECO:0000313|Proteomes:UP000094501};
RN   [1] {ECO:0000313|EMBL:ODS00931.1, ECO:0000313|Proteomes:UP000094501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-67174 {ECO:0000313|EMBL:ODS00931.1,
RC   ECO:0000313|Proteomes:UP000094501};
RX   PubMed=27501305;
RA   Vekeman B., Kerckhof F.M., Cremers G., de Vos P., Vandamme P.,
RA   Boon N., Op den Camp H.J., Heylen K.;
RT   "New Methyloceanibacter diversity from North Sea sediments includes
RT   methanotroph containing solely the soluble methane monooxygenase.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-
CC         N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH;
CC         Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-
CC         COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100;
CC         EC=1.8.1.4; Evidence={ECO:0000256|RuleBase:RU003692};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3,
CC         ECO:0000256|RuleBase:RU003692};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3,
CC       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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ODS00931.1}.
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DR   EMBL; LPWG01000003; ODS00931.1; -; Genomic_DNA.
DR   RefSeq; WP_069436196.1; NZ_LPWG01000003.1.
DR   EnsemblBacteria; ODS00931; ODS00931; AUC68_13470.
DR   Proteomes; UP000094501; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
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   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000094501};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003692};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094501}.
FT   DOMAIN        7    329       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      350    458       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     183    190       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    448    448       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      53     53       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     116    116       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000350-
FT                                3}.
FT   BINDING     206    206       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     274    274       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     314    314       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     44     49       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   469 AA;  49785 MW;  ED2D9A9E201B3098 CRC64;
     MTSATDFDLV VIGGGPGGYV AAIRAAQLGL RTAVVEREHL GGICLNWGCI PTKALLRTSE
     LYRQIKEAEA FGLRVDGVGF DFERLVRRSR DVAGKLARGV AYLMKKNKIA VFDATGRLEG
     PGRVALAGHD GTTLPSLTAS HIIVATGARA RSLPGLEPDG TRIWTYKEAM VPDRLPQSLL
     VIGSGAIGIE FASFYSALGA AVTVVEVQDR ILPVEDEEIS KLAHTAFVKQ RLTIHTSATV
     EQLRDTETGV SARLRTADGN TTEMAVERVI LAVGITGNVE GLGLEEQGVK IDRGHIVVDA
     WCRTGVPGLY AIGDVVGPPW LAHKAMHEGV LCVEKIAGAK AVHPLDPASV PGCTYCTPQI
     ASLGLTERAA REAGYELKIG RYPYAANGKA IALGETDGLV KTIFDAKTGA LLGAHMIGAE
     VTELIQGFAI GKTLETTEAE LMATIFPHPT LSEMMHESVL DAFGRALHI
//
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