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Database: UniProt
Entry: A0A109QDV2_9BACL
LinkDB: A0A109QDV2_9BACL
Original site: A0A109QDV2_9BACL 
ID   A0A109QDV2_9BACL        Unreviewed;       459 AA.
AC   A0A109QDV2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   03-JUL-2019, entry version 21.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   Name=acoL {ECO:0000313|EMBL:AMA72069.1};
GN   ORFNames=ACH33_03880 {ECO:0000313|EMBL:AMA72069.1};
OS   Aneurinibacillus sp. XH2.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA72069.1, ECO:0000313|Proteomes:UP000065566};
RN   [1] {ECO:0000313|EMBL:AMA72069.1, ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|EMBL:AMA72069.1,
RC   ECO:0000313|Proteomes:UP000065566};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMA72069.1, ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|EMBL:AMA72069.1,
RC   ECO:0000313|Proteomes:UP000065566};
RA   Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT   "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT   Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao
RT   oilfield in China.";
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; CP014140; AMA72069.1; -; Genomic_DNA.
DR   EnsemblBacteria; AMA72069; AMA72069; ACH33_03880.
DR   KEGG; anx:ACH33_03880; -.
DR   KO; K00382; -.
DR   Proteomes; UP000065566; Chromosome.
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:UP000065566};
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:UP000065566}.
FT   DOMAIN        3    321       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      340    448       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     178    185       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    438    438       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      48     48       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     201    201       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     266    266       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     306    306       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     39     44       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   459 AA;  49393 MW;  A9FDBB3474A0B0C0 CRC64;
     MSTVTIIGGG PAGYVAAITA ARLGKQVVLV EEAKLGGTCL NEGCMPTKSL LESAETYDRI
     KHASRFGIDL PLDQVHLNWK SVQQYKNNVV KKLVLGIGYL MKKNKVRVVK GKASFLTDHL
     IRVHTEDGIE EITADQFIIA TGAEPIALPF APFDGEWVIH NGHAIALPEV PSSLLIVGGG
     VIGCEFASVY SRMGSKVTIV EMADQILPGE DSDIAAILHQ QLAKDGVLIH TSTSVQEIDR
     NERSVTLAMN GEITKITADY VLVSIGRKPR VEGLGLDQIG VLYTKQGIQV NEHMQTSIPH
     IYACGDVVGG IQLAHFAFHE GEVAAENACG KQKKVNPRVV PRCIYTWPEI GSVGLTEKKA
     REIYGDIRIG EFPFAANGKA LILGEQTGKV KVIVHPEFNE IIGFSIVGPR ATELIGQGAM
     MLHSEMTVDT MEGFIAAHPT LSEALQEAVL SATGLAVHL
//
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