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Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (LPD) (E3 component of pyruvate complex)

 DLDH_SYNY3              Reviewed;         474 AA.
P72740; Q53395;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 138.
RecName: Full=Dihydrolipoyl dehydrogenase;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
Short=LPD;
AltName: Full=E3 component of pyruvate complex;
Name=lpdA; Synonyms=pdhD; OrderedLocusNames=slr1096;
Synechocystis sp. (strain PCC 6803 / Kazusa).
Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
Synechocystis.
NCBI_TaxID=1111708;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PCC 6803 / Kazusa;
PubMed=8905231; DOI=10.1093/dnares/3.3.109;
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium
Synechocystis sp. strain PCC6803. II. Sequence determination of the
entire genome and assignment of potential protein-coding regions.";
DNA Res. 3:109-136(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, AND
CHARACTERIZATION.
PubMed=9387233; DOI=10.1099/00221287-143-11-3543;
Engels A., Pistorius E.K.;
"Characterization of a gene encoding dihydrolipoamide dehydrogenase of
the cyanobacterium Synechocystis sp. strain PCC 6803.";
Microbiology 143:3543-3553(1997).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-
ketoacid dehydrogenase complexes.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Periplasmic side
{ECO:0000250}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA16755.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; BA000022; BAA16755.1; ALT_INIT; Genomic_DNA.
EMBL; Z48564; CAA88451.1; -; Genomic_DNA.
PIR; S74603; S74603.
ProteinModelPortal; P72740; -.
SMR; P72740; -.
IntAct; P72740; 2.
STRING; 1148.SYNGTS_0179; -.
EnsemblBacteria; BAA16755; BAA16755; BAA16755.
KEGG; syn:slr1096; -.
HOGENOM; HOG000276708; -.
InParanoid; P72740; -.
KO; K00382; -.
OMA; TMSEAVM; -.
PhylomeDB; P72740; -.
Proteomes; UP000001425; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 3.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
Glycolysis; Membrane; NAD; Oxidoreductase; Redox-active center;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9387233}.
CHAIN 2 474 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000068051.
NP_BIND 36 44 FAD. {ECO:0000250}.
NP_BIND 184 188 NAD. {ECO:0000250}.
NP_BIND 275 278 NAD. {ECO:0000250}.
ACT_SITE 459 459 Proton acceptor. {ECO:0000250}.
BINDING 53 53 FAD. {ECO:0000250}.
BINDING 119 119 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 207 207 NAD. {ECO:0000250}.
BINDING 323 323 FAD. {ECO:0000250}.
BINDING 331 331 FAD; via amide nitrogen. {ECO:0000250}.
DISULFID 44 49 Redox-active. {ECO:0000250}.
SEQUENCE 474 AA; 50832 MW; A2EFD28D8D9C69E1 CRC64;
MSQDFDYDLV IIGAGVGGHG AALHAVKCGL KTAIIEAKDM GGTCVNRGCI PSKALLAASG
RVREMSDQDH LQQLGIQING VTFTREAIAA HANDLVSKIQ SDLTNSLTRL KVDTIRGWGK
VSGPQEVTVI GDNETRILKA KEIMLCPGSV PFVPPGIEID HKTVFTSDEA VKLETLPQWI
AIIGSGYIGL EFSDVYTALG CEVTMIEALP DLMPGFDPEI AKIAERVLIK SRDIETYTGV
FATKIKAGSP VEIELTDAKT KEVIDTLEVD ACLVATGRIP ATKNLGLETV GVETDRRGFI
EVNDQMQVIK DGKPVPHLWA VGDATGKMML AHAASGQGVV AVENICGRKT EVDYRAIPAA
AFTHPEISYV GLTEAQAKEL GEKEGFVVST AKTYFKGNSK ALAEKETDGI AKVVYRQDTG
ELLGAHIIGI HASDLIQEAA QAIADRKSVR ELAFHVHAHP TLSEVLDEAY KRAV


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