DLDH2_PSEAE
ID DLDH2_PSEAE Reviewed; 478 AA.
AC Q9I3D1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of 2-oxoglutarate dehydrogenase complex;
DE AltName: Full=Glycine oxidation system L-factor;
DE AltName: Full=LPD-GLC;
GN Name=lpdG; OrderedLocusNames=PA1587;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Also acts in the glycine cleavage system. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04976.1; -; Genomic_DNA.
DR PIR; A83449; A83449.
DR RefSeq; NP_250278.1; NC_002516.2.
DR RefSeq; WP_003087422.1; NZ_QZGE01000003.1.
DR PDB; 5U8U; X-ray; 1.35 A; A/B/C/D=1-478.
DR PDBsum; 5U8U; -.
DR AlphaFoldDB; Q9I3D1; -.
DR SMR; Q9I3D1; -.
DR STRING; 287.DR97_302; -.
DR PaxDb; Q9I3D1; -.
DR PRIDE; Q9I3D1; -.
DR EnsemblBacteria; AAG04976; AAG04976; PA1587.
DR GeneID; 882090; -.
DR KEGG; pae:PA1587; -.
DR PATRIC; fig|208964.12.peg.1646; -.
DR PseudoCAP; PA1587; -.
DR HOGENOM; CLU_016755_0_1_6; -.
DR InParanoid; Q9I3D1; -.
DR OMA; CHMIGNY; -.
DR PhylomeDB; Q9I3D1; -.
DR BioCyc; PAER208964:G1FZ6-1617-MON; -.
DR BRENDA; 1.8.1.4; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis;
KW NAD; Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..478
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000287805"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34..49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 188..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 276..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 49..54
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 88..113
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5U8U"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5U8U"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 370..375
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:5U8U"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:5U8U"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:5U8U"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:5U8U"
SQ SEQUENCE 478 AA; 50165 MW; A93C7B03B3C7470F CRC64;
MSQKFDVVVI GAGPGGYVAA IRAAQLGLKT ACIEKYIGKE GKVALGGTCL NVGCIPSKAL
LDSSYKYHEA KEAFKVHGIE AKGVTIDVPA MVARKANIVK NLTGGIATLF KANGVTSFEG
HGKLLANKQV EVTGLDGKTQ VLEAENVIIA SGSRPVEIPP APLTDDIIVD STGALEFQAV
PKKLGVIGAG VIGLELGSVW ARLGAEVTVL EALDKFLPAA DEQIAKEALK VLTKQGLNIR
LGARVTASEV KKKQVTVTFT DANGEQKETF DKLIVAVGRR PVTTDLLAAD SGVTLDERGF
IYVDDHCKTS VPGVFAIGDV VRGAMLAHKA SEEGVMVAER IAGHKAQMNY DLIPSVIYTH
PEIAWVGKTE QTLKAEGVEV NVGTFPFAAS GRAMAANDTT GLVKVIADAK TDRVLGVHVI
GPSAAELVQQ GAIGMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGHAI HIANRKKR
