(data stored in ACNUC8465 zone)

SWISSPROT: B6HE42_PENRW

ID   B6HE42_PENRW            Unreviewed;       512 AA.
AC   B6HE42;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE            EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN   ORFNames=Pc20g04720 {ECO:0000313|EMBL:CAP85801.1}, PCH_Pc20g04720
GN   {ECO:0000313|EMBL:CAP85801.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85801.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85801.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC       {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   -!- 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; AM920435; CAP85801.1; -; Genomic_DNA.
DR   RefSeq; XP_002563014.1; XM_002562968.1.
DR   ProteinModelPortal; B6HE42; -.
DR   STRING; 500485.XP_002563014.1; -.
DR   EnsemblFungi; CAP85801; CAP85801; PCH_Pc20g04720.
DR   GeneID; 8314569; -.
DR   KEGG; pcs:Pc20g04720; -.
DR   eggNOG; KOG1335; Eukaryota.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; TMSEAVM; -.
DR   OrthoDB; EOG092C1XBY; -.
DR   BioCyc; PCHR:PC20G04720-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:EnsemblFungi.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0009353; C:mitochondrial oxoglutarate dehydrogenase complex; IEA:EnsemblFungi.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IEA:EnsemblFungi.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:EnsemblFungi.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:EnsemblFungi.
DR   GO; GO:0004738; F:pyruvate dehydrogenase activity; IEA:EnsemblFungi.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0042743; P:hydrogen peroxide metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006550; P:isoleucine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006574; P:valine catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR006258; Lipoamide_DH.
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   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;
DR   PRODOM; B6HE42.
DR   SWISS-2DPAGE; B6HE42.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   FAD {ECO:0000256|RuleBase:RU003692};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003692};
KW   NAD {ECO:0000256|RuleBase:RU003692};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003692};
KW   Redox-active center {ECO:0000256|RuleBase:RU003692};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT   DOMAIN       48    374       FAD/NAD-binding_dom. {ECO:0000259|Pfam:
FT                                PF07992}.
FT   DOMAIN      393    502       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
SQ   SEQUENCE   512 AA;  54338 MW;  D2AA66323254F01F CRC64;
     MFRAVLPRAT PRSALRHAGP RAIPNNFATS MIFIGQSKRG FASEAGDHDL VIIGGGVAGY
     VAAIKAGQEG LKTACIEKRG KLGGTCLNVG CIPSKSLLNN SHLYHQVLHD TKKRGIEVGD
     VKLNLTQMMK AKDTSVDGLT KGIEFLLKKN GVDYVKGAGS FVDANTIKVA LNEGGEQTLR
     AKNIIIATGS EATGFPGLNI DEKRIITSTG ALALTEVPKK MTVIGGGIIG LEMASVWSRL
     GAEVTVVEFL GQIGGPGMDA EIAKQAQKIL GKQGIKFKTG TKVVSGDDSG STISLNIEAA
     KGGKEEVLDA DVVLVAIGRR PYTEGLNLEQ VGIEKDDRGR LVIDQEYRTK LPHIRVVGDC
     TFGPMLAHKA EEEAVAAIEY IKTGYGHVNY AAIPSVMYTH PEVAWVGQNE AEIKASGVKY
     RVGSFPFSAN SRAKTNLDTE GVVKFIADAE TDRVLGVHII GPGAGEMIAE ATLAIEYGAS
     SEDIARTCHA HPTLSEAFKE AAMATYSKPI HF
//

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