UniProt: A0AW69

Database: UniProt
Entry: A0AW69_ARTS2

LinkDB:  A0AW69_ARTS2 
Original site:  A0AW69_ARTS2

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG GENES (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (22)   

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ID   A0AW69_ARTS2            Unreviewed;       455 AA.
AC   A0AW69;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|ARBA:ARBA00012608, ECO:0000256|RuleBase:RU003692};
GN   OrderedLocusNames=Arth_4200 {ECO:0000313|EMBL:ABK05841.1}, Arth_4300
GN   {ECO:0000313|EMBL:ABK05737.1}, Arth_4469
GN   {ECO:0000313|EMBL:ABK05639.1};
OS   Arthrobacter sp. (strain FB24).
OG   Plasmid 1 {ECO:0000313|EMBL:ABK05639.1},
OG   Plasmid 2 {ECO:0000313|EMBL:ABK05737.1},
OG   Plasmid 3 {ECO:0000313|EMBL:ABK05841.1},
OG   Plasmid FB24-1 {ECO:0000313|Proteomes:UP000000754},
OG   Plasmid FB24-2 {ECO:0000313|Proteomes:UP000000754}, and
OG   Plasmid FB24-3 {ECO:0000313|Proteomes:UP000000754}.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=290399 {ECO:0000313|EMBL:ABK05639.1, ECO:0000313|Proteomes:UP000000754};
RN   [1] {ECO:0000313|EMBL:ABK05639.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   PLASMID=1 {ECO:0000313|EMBL:ABK05639.1}, and FB24
RC   {ECO:0000313|EMBL:ABK05639.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.;
RT   "Complete sequence of plasmid 1 of Arthrobacter sp. FB24.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABK05737.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   PLASMID=2 {ECO:0000313|EMBL:ABK05737.1}, and FB24
RC   {ECO:0000313|EMBL:ABK05737.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.;
RT   "Complete sequence of plasmid 2 of Arthrobacter sp. FB24.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABK05841.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   PLASMID=3 {ECO:0000313|EMBL:ABK05841.1}, and FB24
RC   {ECO:0000313|EMBL:ABK05841.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.;
RT   "Complete sequence of plasmid 3 of Arthrobacter sp. FB24.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000000754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24 {ECO:0000313|Proteomes:UP000000754};
RC   PLASMID=FB24-1 {ECO:0000313|Proteomes:UP000000754}, FB24-2
RC   {ECO:0000313|Proteomes:UP000000754}, and FB24-3
RC   {ECO:0000313|Proteomes:UP000000754};
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C., Brettin T.,
RA   Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC         N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC         Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83100; EC=1.8.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00043836,
CC         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|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003692}.
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DR   EMBL; CP000455; ABK05639.1; -; Genomic_DNA.
DR   EMBL; CP000456; ABK05737.1; -; Genomic_DNA.
DR   EMBL; CP000457; ABK05841.1; -; Genomic_DNA.
DR   RefSeq; WP_011689645.1; NC_008539.1.
DR   AlphaFoldDB; A0AW69; -.
DR   KEGG; art:Arth_4200; -.
DR   KEGG; art:Arth_4300; -.
DR   KEGG; art:Arth_4469; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_2_11; -.
DR   Proteomes; UP000000754; Plasmid FB24-1.
DR   Proteomes; UP000000754; Plasmid FB24-2.
DR   Proteomes; UP000000754; Plasmid FB24-3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   NCBIfam; TIGR01350; lipoamide_DH; 1.
DR   PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003692}; Plasmid {ECO:0000313|EMBL:ABK05639.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000754}.
FT   DOMAIN          3..314
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          334..443
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        432
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         112
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         136..138
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         172..179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        40..45
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   455 AA;  47702 MW;  07C4CD4B382A059D CRC64;
     MTYDLVILGG GSAGYAAALR GAQLGMTVAL IEGDKLGGTC LHRGCIPTKA LLHSAEVADT
     IRESEAFGVE SAFGRVDMAG VTKFKASVVD RLYKGLQGLV SSRSVDLIQG WGTLAAADTV
     EVDGTSYRGK NIVLATGSYS KSLPGLDISG RVITSEQALE MDFVPKSALI LGGGVIGVEF
     ASVWASFGTE VTIIEALPRL IANEDESLSK GLQRAFTKRG IKFLTNTMFA GVSQNDDGVT
     VTTQDDKTLE AEVLLVAVGR GPVTAKLGYE DAGIPMERGF VPTNDRLHTG VGNVYAIGDI
     VPGLQLAHRG FQQGIFVAEE IAGLSPAPII ESGIPRVTYS EPQAGSVGLT EAQAKEQFSA
     DGIETVEYNL GGNAKSQMLQ TAGFIKLIRQ KEGPIIGVHM LGARVSELIG EGQLMVNWEA
     YPEDVASLLH AHPTQNDAIG EAALALAGKP LHAHG
//

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