UniProt: A0A0P7GMH0

Database: UniProt
Entry: A0A0P7GMH0_9EURY

LinkDB:  A0A0P7GMH0_9EURY 
Original site:  A0A0P7GMH0_9EURY

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (16)   

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ID   A0A0P7GMH0_9EURY        Unreviewed;       474 AA.
AC   A0A0P7GMH0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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   Name=lpdA_1 {ECO:0000313|EMBL:KPN29761.1};
GN   ORFNames=SY89_00478 {ECO:0000313|EMBL:KPN29761.1};
OS   Halolamina pelagica.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae.
OX   NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN29761.1, ECO:0000313|Proteomes:UP000050535};
RN   [1] {ECO:0000313|Proteomes:UP000050535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA   Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA   Schwartz K.J., Yoon K.;
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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|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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPN29761.1}.
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DR   EMBL; LGUC01000001; KPN29761.1; -; Genomic_DNA.
DR   RefSeq; WP_054582966.1; NZ_LGUC01000001.1.
DR   AlphaFoldDB; A0A0P7GMH0; -.
DR   STRING; 699431.SY89_00478; -.
DR   PATRIC; fig|699431.3.peg.498; -.
DR   OrthoDB; 27922at2157; -.
DR   Proteomes; UP000050535; Unassembled WGS sequence.
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:SF160; DIHYDROLIPOYL DEHYDROGENASE; 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|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003692}; Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050535}.
FT   DOMAIN          11..333
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          352..461
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   474 AA;  49806 MW;  B2C6EED66A06422A CRC64;
     MVVGDVTTGT EVLVIGAGPG GYVAAIRAAQ NGLDTTLVDR DGYGGTCLNY GCIPSKALIS
     ATDVAHDARN ATEMGVHADP VIHTDEMQEW KDGVVDQLTG GVEKLCKANG VNLMQGEATF
     VDDSTARIAH GGEGQGSESI DFEHAIVATG SRPIQVPGFE FEHDPIWSSR DALEVEEPPE
     KLLVVGAGYI GMELSTVFAK LGVDVTVVEM LDGIMPGYED DVTRPVKKRA DELGIEFNFG
     EAASDWEETE GGVVVTTEDE DGAEYTYDAD KMLVAVGRQP ISESLDPEAA GVEVDENGFI
     QTDDQARTNV DNIYAVGDVA GEPMLAHKAS KEGIVAAEVI AGEPAALDQQ AIPAAVFTDP
     EIATVGMTEA EAEEAGFEPK IGQFPFRASG RALSTGESEG FVRLVAEQEA GFILGAQIVG
     PEASELIAEC ALAIEMGATL EDVASTVHTH PTLAEAVMEA AENANDEAIH TLNR
//

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