(data stored in ACNUC7421 zone)

HOGENOM: THICR_1_PE1003

ID   THICR_1_PE1003                       STANDARD;      PRT;   594 AA.
AC   THICR_1_PE1003; Q31GX5;
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; EC=1.8.1 4;
DE   (THICR_1.PE1003).
GN   OrderedLocusNames=Tcr_1003;
OS   THIOMICROSPIRA CRUNOGENA XCL-2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=317025;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THICR_1.PE1003.
CC       Thiomicrospira crunogena XCL-2, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q31GX5_THICR
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; Q31GX5; -.
DR   EMBL; CP000109; ABB41598.1; -; Genomic_DNA.
DR   RefSeq; YP_391272.1; NC_007520.2.
DR   ProteinModelPortal; Q31GX5; -.
DR   SMR; Q31GX5; 123-592.
DR   STRING; Q31GX5; -.
DR   GeneID; 3760489; -.
DR   GenomeReviews; CP000109_GR; Tcr_1003.
DR   KEGG; tcx:Tcr_1003; -.
DR   NMPDR; fig|317025.3.peg.789; -.
DR   eggNOG; COG1249; -.
DR   OMA; MDENSAQ; -.
DR   PhylomeDB; Q31GX5; -.
DR   ProtClustDB; CLSK2772645; -.
DR   BioCyc; TCRU317025:TCR_1003-MONOMER; -.
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; 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   PANTHER; PTHR22912:SF20; Lipoamide_DH; 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; THICR_1.PE1003; -.
KW   dihydrolipoamide dehydrogenase;
KW   Complete proteome; Lipoyl; Oxidoreductase.
SQ   SEQUENCE   594 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSKIVDILIP DIGDFAEVDV IEVLVSAGEE IIQDDSLLTL ESDKATMEIP APYAGRVVEM
     NVDVGDKVKE GSVVGKIEIA DVETVSSNVE ESVTPEPTPE KTDQKTTETP APKAVSAADL
     PDADMQCDVL VLGSGPGGYT AAFRAADLGK KVVMIERYES IGGVCLNVGC IPSKALLHMS
     VVLNETREMG AHGIEFAEPK IDTNKMRAFK DSVIGKLTGG LSGLAKARNV DVVQGYGKFS
     SANTVTVDLA DGGTKTIAFE NAIIAAGSRV VKLPFIPHDD PRVMDSTDAL ELEEVPKRML
     VIGGGIIGLE MAQVYDSLGS NITVVELGDT IIPGADKDIS KPLLRRIKKK YENIYLKSKV
     TNVEAKEEGL VVTFEGKDCP ETDTFDRILV AVGRAPNGKL IDAEKAGVAV NDWGFIEVDE
     RQKTNVDHIY AIGDIVGQPM LAHKAVHEGK VAAEVINGMP SAFTPMGIPS VAYTDPEVAW
     AGKTEDELKA EGIEYEKGAF PWAASGRSLS LGRDEGLTKA LFCAETHRLL GCGIVGPNAG
     ELVAEAMLAI EMGADMQDIG LTIHPHPTLS ETLCFAAEMA EGTITDLMPP KKKK
//

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