ID A7IBM5_XANP2 Unreviewed; 467 AA.
AC A7IBM5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 01-MAY-2013, entry version 43.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
GN OrderedLocusNames=Xaut_0159;
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.,
RA Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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.
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DR EMBL; CP000781; ABS65418.1; -; Genomic_DNA.
DR RefSeq; YP_001415075.1; NC_009720.1.
DR ProteinModelPortal; A7IBM5; -.
DR SMR; A7IBM5; 2-467.
DR STRING; 78245.Xaut_0159; -.
DR EnsemblBacteria; ABS65418; ABS65418; Xaut_0159.
DR GeneID; 5423247; -.
DR KEGG; xau:Xaut_0159; -.
DR PATRIC; 24042282; VBIXanAut29526_0452.
DR eggNOG; COG1249; -.
DR HOGENOM; HOG000276708; -.
DR KO; K00382; -.
DR OMA; HIVGFGA; -.
DR ProtClustDB; PRK06292; -.
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 Gene3D; 3.30.390.30; -; 1.
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 PANTHER; PTHR22912:SF20; PTHR22912:SF20; 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.
PE 3: Inferred from homology;
KW Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Redox-active center.
SQ SEQUENCE 467 AA; 48513 MW; 91198215F83E3911 CRC64;
MSYDLTIIGT GPGGYVCAIR AAQLGLKVAV VEKRGTHGGT CLNVGCIPSK ALLYASELFE
EAGHKFGEMG IGVPAPKLDL KAMLAFKDKG VDGNVKGVEF LLKKNKVDVY MGAGKILGTG
KVEVTLNADG KVEVLETKNI VIATGSDVAP LPGVTIDEQR IVSSTGALSL PKVPGKLLVV
GAGVIGLELG SVWRRLGAQV TVVEFLDRIL PGMDSDVAKS FQRILDKQGF AFKLGTKVTG
VDTSGKTLKV SVEPAAGGAA EVIEADVVLV AIGRIPYTAG LGLDEAGVAK DGRGRVVTDH
HFATNVPGIY AIGDVIVGPM LAHKAEDEGV ALAELLAGKA GHVNYDVIPG VVYTFPEVAS
VGKSEDDLKA AGVAYKVGKF PFTANGRTKV NNTTDGFVKI IADAATDKVL GAHIIGPEAG
EMIHECAVLM EFGGSSEDLA RTCHAHPTRS EAVKEAAMAV EKRAIHM
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