Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of 2-oxoglutarate dehydrogenase complex) (Glycine oxidation system L-factor) (LPD-GLC)

 DLDH2_PSEAE             Reviewed;         478 AA.
Q9I3D1;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 107.
RecName: Full=Dihydrolipoyl dehydrogenase;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=E3 component of 2-oxoglutarate dehydrogenase complex;
AltName: Full=Glycine oxidation system L-factor;
AltName: Full=LPD-GLC;
Name=lpdG; OrderedLocusNames=PA1587;
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=208964;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
1C / PRS 101 / PAO1;
PubMed=10984043; DOI=10.1038/35023079;
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an
opportunistic pathogen.";
Nature 406:959-964(2000).
-!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex
catalyzes the overall conversion of alpha-keto acids to acyl-CoA
and CO(2). It contains multiple copies of 3 enzymatic components:
branched-chain alpha-keto acid decarboxylase (E1), lipoamide
acyltransferase (E2) and lipoamide dehydrogenase (E3) (By
similarity). {ECO:0000250}.
-!- FUNCTION: Also acts in the glycine cleavage system. {ECO:0000250}.
-!- 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: Cytoplasm {ECO:0000250}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AE004091; AAG04976.1; -; Genomic_DNA.
PIR; A83449; A83449.
RefSeq; NP_250278.1; NC_002516.2.
RefSeq; WP_003087422.1; NC_002516.2.
PDB; 5U8U; X-ray; 1.35 A; A/B/C/D=1-478.
PDBsum; 5U8U; -.
ProteinModelPortal; Q9I3D1; -.
SMR; Q9I3D1; -.
STRING; 208964.PA1587; -.
PaxDb; Q9I3D1; -.
PRIDE; Q9I3D1; -.
EnsemblBacteria; AAG04976; AAG04976; PA1587.
GeneID; 882090; -.
KEGG; pae:PA1587; -.
PATRIC; fig|208964.12.peg.1646; -.
PseudoCAP; PA1587; -.
eggNOG; ENOG4107QN2; Bacteria.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276708; -.
InParanoid; Q9I3D1; -.
KO; K00382; -.
OMA; CHMIGNY; -.
PhylomeDB; Q9I3D1; -.
BRENDA; 1.8.1.4; 5087.
Proteomes; UP000002438; Chromosome.
GO; GO:0005737; C:cytoplasm; 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:0020012; P:evasion or tolerance of host immune response; IDA:PseudoCAP.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IDA:PseudoCAP.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 3.
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; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Disulfide bond; FAD;
Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center;
Reference proteome.
CHAIN 1 478 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000287805.
NP_BIND 34 49 FAD. {ECO:0000250}.
NP_BIND 188 192 NAD. {ECO:0000250}.
NP_BIND 276 279 NAD. {ECO:0000250}.
ACT_SITE 451 451 Proton acceptor. {ECO:0000250}.
BINDING 58 58 FAD. {ECO:0000250}.
BINDING 122 122 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 211 211 NAD. {ECO:0000250}.
BINDING 245 245 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 319 319 FAD. {ECO:0000250}.
BINDING 327 327 FAD; via amide nitrogen. {ECO:0000250}.
DISULFID 49 54 Redox-active. {ECO:0000250}.
STRAND 4 10 {ECO:0000244|PDB:5U8U}.
HELIX 14 25 {ECO:0000244|PDB:5U8U}.
STRAND 30 34 {ECO:0000244|PDB:5U8U}.
STRAND 41 43 {ECO:0000244|PDB:5U8U}.
HELIX 47 52 {ECO:0000244|PDB:5U8U}.
HELIX 54 72 {ECO:0000244|PDB:5U8U}.
HELIX 75 77 {ECO:0000244|PDB:5U8U}.
STRAND 82 86 {ECO:0000244|PDB:5U8U}.
HELIX 88 113 {ECO:0000244|PDB:5U8U}.
STRAND 116 124 {ECO:0000244|PDB:5U8U}.
HELIX 126 128 {ECO:0000244|PDB:5U8U}.
STRAND 129 133 {ECO:0000244|PDB:5U8U}.
STRAND 139 149 {ECO:0000244|PDB:5U8U}.
STRAND 153 155 {ECO:0000244|PDB:5U8U}.
TURN 165 167 {ECO:0000244|PDB:5U8U}.
HELIX 171 174 {ECO:0000244|PDB:5U8U}.
STRAND 182 187 {ECO:0000244|PDB:5U8U}.
HELIX 191 202 {ECO:0000244|PDB:5U8U}.
STRAND 206 210 {ECO:0000244|PDB:5U8U}.
STRAND 212 217 {ECO:0000244|PDB:5U8U}.
HELIX 222 234 {ECO:0000244|PDB:5U8U}.
STRAND 237 240 {ECO:0000244|PDB:5U8U}.
STRAND 244 251 {ECO:0000244|PDB:5U8U}.
STRAND 254 261 {ECO:0000244|PDB:5U8U}.
STRAND 264 275 {ECO:0000244|PDB:5U8U}.
STRAND 279 281 {ECO:0000244|PDB:5U8U}.
TURN 284 286 {ECO:0000244|PDB:5U8U}.
STRAND 314 316 {ECO:0000244|PDB:5U8U}.
HELIX 318 320 {ECO:0000244|PDB:5U8U}.
STRAND 321 323 {ECO:0000244|PDB:5U8U}.
HELIX 327 341 {ECO:0000244|PDB:5U8U}.
STRAND 355 357 {ECO:0000244|PDB:5U8U}.
STRAND 359 361 {ECO:0000244|PDB:5U8U}.
STRAND 363 367 {ECO:0000244|PDB:5U8U}.
HELIX 370 375 {ECO:0000244|PDB:5U8U}.
STRAND 380 386 {ECO:0000244|PDB:5U8U}.
HELIX 387 389 {ECO:0000244|PDB:5U8U}.
HELIX 391 395 {ECO:0000244|PDB:5U8U}.
STRAND 402 408 {ECO:0000244|PDB:5U8U}.
TURN 409 411 {ECO:0000244|PDB:5U8U}.
STRAND 413 421 {ECO:0000244|PDB:5U8U}.
HELIX 424 436 {ECO:0000244|PDB:5U8U}.
HELIX 441 445 {ECO:0000244|PDB:5U8U}.
HELIX 456 465 {ECO:0000244|PDB:5U8U}.
STRAND 470 472 {ECO:0000244|PDB:5U8U}.
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


Related products :

Catalog number Product name Quantity
EIAAB28679 2-oxoglutarate dehydrogenase complex component E2,Bos taurus,Bovine,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransfera
18-783-77883 RABBIT ANTI PORCINE LIPOAMIDE DEHYDROGENASE - EC 1.8.1.4; Dihydrolipoamide dehydrogenase; Pyruvate dehydrogenase complex E3 subunit; PDC-E3; E3; Glycine cleavage system L protein Polyclonal 1 ml
EIAAB11372 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,GCSL,Glycine cleavage system L protein,Homo sapiens,Human,LAD,PHE3
27-169 DLD is the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketogl 0.05 mg
EIAAB28675 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28676 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28678 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28677 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
E1923b ELISA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
U1923b CLIA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
U1923b CLIA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
E1923b ELISA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Bos taurus,Bovine,OGDC-E1,OGDH 96T
U1923r CLIA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,OGDC-E1,Ogdh,Ogdhl,Rat,Rattus norvegicus 96T
U1923m CLIA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 96T
U1923r CLIA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,OGDC-E1,Ogdh,Ogdhl,Rat,Rattus norvegicus 96T
U1923h CLIA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Homo sapiens,Human,OGDC-E1,OGDH 96T
U1923h CLIA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Homo sapiens,Human,OGDC-E1,OGDH 96T
E1923r ELISA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,OGDC-E1,Ogdh,Ogdhl,Rat,Rattus norvegicus 96T
E1923m ELISA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 96T
EIAAB28707 2-oxoglutarate dehydrogenase complex component E1-like,2-oxoglutarate dehydrogenase-like, mitochondrial,Alpha-ketoglutarate dehydrogenase-like,Homo sapiens,Human,KIAA1290,OGDC-E1-like,OGDHL
E1923m ELISA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 96T
E1923r ELISA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,OGDC-E1,Ogdh,Ogdhl,Rat,Rattus norvegicus 96T
E1923h ELISA kit 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Homo sapiens,Human,OGDC-E1,OGDH 96T
E1923h ELISA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Homo sapiens,Human,OGDC-E1,OGDH 96T
U1923m CLIA 2-oxoglutarate dehydrogenase complex component E1,2-oxoglutarate dehydrogenase, mitochondrial,Alpha-ketoglutarate dehydrogenase,Kiaa4192,Mouse,Mus musculus,OGDC-E1,Ogdh 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur