(data stored in ACNUC7421 zone)

HOGENOM: ALKOO_1_PE1014

ID   ALKOO_1_PE1014                       STANDARD;      PRT;   572 AA.
AC   ALKOO_1_PE1014; A8MG46;
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   SubName: Full=Dihydrolipoamide dehydrogenase; (ALKOO_1.PE1014).
GN   OrderedLocusNames=Clos_1037;
OS   ALKALIPHILUS OREMLANDII OHILAS.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=350688;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ALKOO_1.PE1014.
CC       Alkaliphilus oremlandii OhILAs, complete genome.
CC       pAACI03, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:A8MG46_ALKOO
CC   -!- COFACTOR: Binds 1 lipoyl cofactor covalently (By similarity).
CC   -!- SIMILARITY: Contains 1 lipoyl-binding domain.
CC   -!- GENE_FAMILY: HOG000276708 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8MG46; -.
DR   EMBL; CP000853; ABW18584.1; -; Genomic_DNA.
DR   RefSeq; YP_001512580.1; NC_009922.1.
DR   ProteinModelPortal; A8MG46; -.
DR   STRING; A8MG46; -.
DR   GeneID; 5677987; -.
DR   GenomeReviews; CP000853_GR; Clos_1037.
DR   KEGG; aoe:Clos_1037; -.
DR   OMA; KAQAIGH; -.
DR   ProtClustDB; CLSK912270; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
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   InterPro; IPR011053; Single_hybrid_motif.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 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   SUPFAM; SSF51230; Hybrid_motif; 1.
DR   TIGRFAMs; TIGR01350; Lipoamide_DH; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
DR   HOGENOMDNA; ALKOO_1.PE1014; -.
KW   dihydrolipoamide dehydrogenase;
KW   Complete proteome; Lipoyl.
SQ   SEQUENCE   572 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIVEVKLEKL SGHNKSGVIG SIHKKSGDIV KVGEEIFDIE AKKGNITITS DVEGEIVEIK
     VKEGDPVSIG DVLLMVEGEK ADSKGEANKK QGFNYMANFL KPQKESMDSD IVIIGGGPGG
     YVAAIEGAKQ GAKVILIEKE ELGGTCLNRG CIPTKALVRS SEVYELVKNS AEYGVFNSSS
     SYDFSKIIAR KNDIVNELVG GIDYLLSKNN VTVLKGSGEI LDKNTVFVKE KNKEITINTN
     NIIIATGSKA FVPPIKGAAS KNIVTSKEML NLSELPQKII IVGGGVIGME FAFICNALDT
     DVSVVEFAED ILVALDEDVR TEIREIAIEK GIKIYTSSKV EEIIDTEEGQ SIVVFDKNGT
     KGYITGDKVL MSVGRVPFYG DIDLEKLGID LNEKGRGIKV NSKMQTTVDN IYAIGDVTNI
     IQLAHVASHQ GIIAIENILG KDVEANYEVV PSAIFTSPEI ASVGIHEKAA MEQGISVKTG
     KFPFGANGKA LTQGERRGFV KIITEEATGV ILGGSIIGPH ATDLIHEVAV AIQNKLTAEQ
     LINTIHAHPT TAEAVHEALL ATTPKGAIHF AE
//

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