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Database: UniProt
Entry: A3SJV9_ROSNI
LinkDB: A3SJV9_ROSNI
Original site: A3SJV9_ROSNI 
ID   A3SJV9_ROSNI            Unreviewed;       462 AA.
AC   A3SJV9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   03-JUL-2019, entry version 77.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   ORFNames=ISM_05085 {ECO:0000313|EMBL:EAP77640.1};
OS   Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseovarius.
OX   NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP77640.1, ECO:0000313|Proteomes:UP000005954};
RN   [1] {ECO:0000313|EMBL:EAP77640.1, ECO:0000313|Proteomes:UP000005954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC   {ECO:0000313|Proteomes:UP000005954};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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:EAP77640.1}.
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DR   EMBL; AALY01000001; EAP77640.1; -; Genomic_DNA.
DR   RefSeq; WP_009813041.1; NZ_CH724156.1.
DR   STRING; 89187.ISM_05085; -.
DR   EnsemblBacteria; EAP77640; EAP77640; ISM_05085.
DR   eggNOG; ENOG4107QN2; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   OrthoDB; 267896at2; -.
DR   BioCyc; RNUB89187:G11Z7-1028-MONOMER; -.
DR   Proteomes; UP000005954; 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:UP000005954};
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:UP000005954}.
FT   DOMAIN        4    324       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      343    452       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     176    183       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   NP_BIND     315    318       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    441    441       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      51     51       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     115    115       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000350-
FT                                3}.
FT   BINDING     199    199       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     268    268       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     309    309       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     42     47       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   462 AA;  48770 MW;  8D7C787F58BB29C2 CRC64;
     MASYDVIVIG AGPGGYVAAI RCAQLGLKTA CVEGRDTLGG TCLNVGCIPS KALLHASHML
     HEAEHNFAKM GLKGKSPSVD WPGMLAYKDD VIGQNTKGVE FLFKKNKIDW LKGWGSIPEA
     GKVKVGDEVH EAKNIIIASG SEAASLPGVE VDEKIVVTST GALELPKVPK KLVVIGAGVI
     GLELGSVYAR LGSEVTVIEY LDAVTPGMDA EVQKTVQRML KKQGMSFIMG AAVQKTEATK
     TKAKVHYKLR KDDSEHVLDA DVVLVATGRK PYTDGLGLEA LGVEMSQRGQ IKTDDHWQTN
     VKGIYAIGDA IDGPMLAHKA EDEGMAAAEV IAGKAGHVNY GVIPGVIYTH PEVATVGKTE
     DQLKEEGRAY KVGKFSFMGN GRAKAVFAGD GFVKLLADKD TDRILGCHII GPGAGDLIHE
     VCVAMEFGAS AEDLAMTCHA HPTYSEAVRE AALACGDGAI HS
//
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