UniProt: A0A0U5GWU2

Database: UniProt
Entry: A0A0U5GWU2_9EURY

LinkDB:  A0A0U5GWU2_9EURY 
Original site:  A0A0U5GWU2_9EURY

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (19)   

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ID   A0A0U5GWU2_9EURY        Unreviewed;       474 AA.
AC   A0A0U5GWU2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-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 {ECO:0000313|EMBL:CQH43856.1};
GN   ORFNames=HHUB_1016 {ECO:0000313|EMBL:CQH43856.1};
OS   Halobacterium hubeiense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH43856.1, ECO:0000313|Proteomes:UP000066737};
RN   [1] {ECO:0000313|Proteomes:UP000066737}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX   PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA   Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA   Yang C., Oksanen H.M., Bamford D.H.;
RT   "The complete genome of a viable archaeum isolated from 123-million-year-
RT   old rock salt.";
RL   Environ. Microbiol. 18:565-579(2016).
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}.
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DR   EMBL; LN831302; CQH43856.1; -; Genomic_DNA.
DR   RefSeq; WP_059055086.1; NZ_LN831302.1.
DR   AlphaFoldDB; A0A0U5GWU2; -.
DR   STRING; 1407499.HHUB_1016; -.
DR   GeneID; 26657727; -.
DR   KEGG; hhb:Hhub_1016; -.
DR   OrthoDB; 27922at2157; -.
DR   Proteomes; UP000066737; Chromosome I.
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:UP000066737}.
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;  49421 MW;  7502C38915A32C77 CRC64;
     MVVGDVSTGT DVAVVGGGPG GYVAAIRAAQ LGLDTTLVEM DAYGGTCLNY GCIPSKALIT
     ATDVAHDAGN AEEMGVYADP DVDFGEMVEW KDGVVDQLTG GVEKLCKASG VNLMEGRAEF
     AGNDKLRVVH GGEGQGSETI EYENCVVATG SRPIEVPGFE FDADPVLDSR QALAMDDLPD
     SIVVVGAGYI GMEISTVLAK LGVDVTVVEM LDEALAGYPD DLTQPVKQRA EELGIDFEFG
     LAADHWEESG DGIVVAAEDE DGELTEFETD KVLVAVGRQP VTDTLNLDAI DLEPNDDGRL
     ETDEQARTDV ENVFAIGDVA PGPMLAHKAS KEGQVAAEVA AGEPAALDYQ AVPAAVFTDP
     EIATVGLTED DAREEGFEPA VGTFPFRASG RALTTGDSDG FVRVVADEES GFLLGAQIVG
     PEASELIAEL GLAIEMGATL EDVASTIHTH PTLSEATMEA AEHALGHAIH TLNR
//

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