(data stored in ACNUC22050 zone)

HOGENOM: LACTH_1_PE115

ID   LACTH_1_PE115                        STANDARD;      PRT;   498 AA.
AC   LACTH_1_PE115; C5DBI9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Dihydrolipoyl dehydrogenase; EC=1.8.1 4; (LACTH_1.PE115).
GN   OrderedLocusNames=KLTH0A02992g;
OS   LACHANCEA THERMOTOLERANS.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=381046;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LACTH_1.PE115.
CC       Kluyveromyces thermotolerans strain CBS6340 chromosome A complete seque
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C5DBI9_LACTC
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
CC   -!- GENE_FAMILY: HOG000276708 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C5DBI9; -.
DR   EMBL; CU928165; CAR21146.1; -; Genomic_DNA.
DR   RefSeq; XP_002551588.1; XM_002551542.1.
DR   ProteinModelPortal; C5DBI9; -.
DR   STRING; C5DBI9; -.
DR   GeneID; 8290387; -.
DR   GenomeReviews; CU928165_GR; KLTH0A02992g.
DR   KEGG; lth:KLTH0A02992g; -.
DR   OrthoDB; EOG43FM59; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   PANTHER; PTHR22912:SF20; Lipoamide_DH; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF55424; FAD/NAD-linked_reductase_dimer; 1.
DR   TIGRFAMs; TIGR01350; Lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
DR   HOGENOMDNA; LACTH_1.PE115; -.
KW   CAR21146.1824841755old_1320000031;
KW   KLTH0A02992p;
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center.
SQ   SEQUENCE   498 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLRMRLQAGA SRRFLSGTSR MLAEKKKHDL VVVGSGPGGY VAAIKAAQLG FDTACVEKRG
     RAGGTCLNVG CIPSKALLNN SHLYHQMKHE AKQRGIDISG DVSVNVAQLQ KAKDTSVKQL
     TGGIEMLFKK NGVTYYKGHG SFEDENNIKV SPVEGVEGSV TEETILEAKN IIVATGSEVT
     PFPGIKIDEE RIVSSTGALS LKEVPKRLAI IGGGIIGLEM GSVYSRLGSK VSVVEFLPKI
     GATMDDEVAS ATQKFLKKQG FDFKLGTKVL SAERNGDVVN IEVENVKSGK KESLEADVLL
     VAIGRRPYIQ GLNAEKLGLE VDKRGRLVID EQFNTKFPHI KVIGDVTFGP MLAHKAEEEG
     IAAVEYLKEG HGHVNYANIP SVMYTHPEVA WVGKTEEQLK EAGISYKIGK FPFMANSRAK
     TNQDSDGFVK ILIDAETERI LGAHIIGPNA GEMIAEAGLA LEYGASAEDV ARVCHAHPTL
     SEAFKEANLA AYSKSINF
//

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