P09622 (DLDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydrolipoyl dehydrogenase, mitochondrial
EC=1.8.1.4

Alternative name(s):
Dihydrolipoamide dehydrogenase
Glycine cleavage system L protein

Gene names

Name:	DLD
Synonyms:	GCSL, LAD, PHE3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.
Catalytic activity	Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds. Ref.12
Subcellular location	Mitochondrion matrix.
Post-translational modification	Tyrosine phosphorylated By similarity.
Involvement in disease	Defects in DLD are involved in the development of congenital infantile lactic acidosis. Maple syrup urine disease (MSUD) [MIM:248600]: Characterized by mental and physical retardation, feeding problems and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine, resulting from a block in oxidative decarboxylation. Note: The disease is caused by mutations affecting the gene represented in this entry.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Sequence caution	The sequence BAD92940.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NAD
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	branched-chain amino acid catabolic process Traceable author statement. Source: Reactome cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome gastrulation Inferred from electronic annotation. Source: Compara lysine catabolic process Traceable author statement. Source: Reactome mitochondrial electron transport, NADH to ubiquinone Inferred from electronic annotation. Source: Compara proteolysis Inferred from electronic annotation. Source: Compara pyruvate metabolic process Traceable author statement. Source: Reactome regulation of acetyl-CoA biosynthetic process from pyruvate Traceable author statement. Source: Reactome regulation of membrane potential Inferred from electronic annotation. Source: Compara sperm capacitation Inferred from electronic annotation. Source: Compara tricarboxylic acid cycle Traceable author statement. Source: Reactome
Cellular_component	acrosomal matrix Inferred from electronic annotation. Source: Compara mitochondrial matrix Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA
Molecular_function	dihydrolipoyl dehydrogenase activity Traceable author statement Ref.15. Source: ProtInc flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

35

Mitochondrion

Chain

36 – 509

474

Dihydrolipoyl dehydrogenase, mitochondrial

PRO_0000030295

Regions

Nucleotide binding

71 – 80

10

FAD

Nucleotide binding

183 – 185

3

FAD

Nucleotide binding

220 – 227

8

NAD

Nucleotide binding

361 – 364

4

FAD

Sites

Active site

487

1

Proton acceptor By similarity

Binding site

89

1

FAD

Binding site

154

1

FAD; via amide nitrogen and carbonyl oxygen

Binding site

243

1

NAD

Binding site

278

1

NAD; via amide nitrogen and carbonyl oxygen

Binding site

314

1

NAD; via amide nitrogen

Binding site

355

1

FAD

Amino acid modifications

Modified residue

127

1

N6-acetyllysine By similarity

Modified residue

143

1

N6-acetyllysine Ref.10

Modified residue

410

1

N6-acetyllysine Ref.10

Modified residue

417

1

N6-acetyllysine Ref.10

Disulfide bond

80 ↔ 85

Redox-active

Natural variations

Natural variant

72

1

K → E in DLD deficiency. Ref.15

VAR_006907

Natural variant

104

1

K → T. Ref.1 Ref.3
Corresponds to variant rs1130477 [ dbSNP | Ensembl ].

VAR_031922

Natural variant

229

1

G → C in DLD deficiency; carrier rate among Askenazi Jewish 1:94. Ref.17

VAR_015820

Natural variant

331

1

L → V.
Corresponds to variant rs17624 [ dbSNP | Ensembl ].

VAR_014555

Natural variant

488

1

P → L in DLD deficiency. Ref.15

VAR_006908

Natural variant

495

1

R → G in DLD deficiency; loss of enzyme activity. Ref.14 Ref.16

VAR_015821

Experimental info

Sequence conflict

154

1

G → R in AAA35764. Ref.2

Sequence conflict

209

1

L → F in BAD92940. Ref.5

Sequence conflict

493

1

A → AEA in AAB01381. Ref.3

Secondary structure

1

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509

Helix Strand Turn

Details...

Beta strand

40 – 47

8

Helix

51 – 62

12

Beta strand

67 – 71

5

Beta strand

73 – 77

5

Helix

78 – 83

6

Helix

85 – 102

18

Helix

105 – 108

4

Beta strand

111 – 114

4

Beta strand

116 – 118

3

Helix

120 – 144

25

Beta strand

148 – 158

11

Beta strand

161 – 165

5

Beta strand

171 – 181

11

Beta strand

185 – 187

3

Beta strand

197 – 201

5

Helix

203 – 206

4

Beta strand

214 – 219

6

Helix

223 – 234

12

Beta strand

238 – 242

5

Beta strand

244 – 249

6

Helix

255 – 267

13

Beta strand

271 – 273

3

Beta strand

275 – 283

9

Beta strand

289 – 295

7

Beta strand

302 – 311

10

Beta strand

315 – 317

3

Helix

324 – 327

4

Beta strand

350 – 352

3

Helix

354 – 356

3

Beta strand

357 – 359

3

Helix

363 – 377

15

Helix

386 – 388

3

Beta strand

391 – 393

3

Beta strand

395 – 403

9

Helix

406 – 412

7

Beta strand

416 – 422

7

Helix

423 – 425

3

Helix

427 – 431

5

Beta strand

438 – 444

7

Turn

445 – 447

3

Beta strand

449 – 457

9

Helix

460 – 473

14

Helix

477 – 482

6

Helix

491 – 503

13

Sequences

	Sequence		Length	Mass (Da)
	P09622 [UniParc]. Last modified November 24, 2009. Version 2. Checksum: 7613492C516F3835	FASTA	509	54,177
	10 20 30 40 50 60 MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA 70 80 90 100 110 120 AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL 130 140 150 160 170 180 DKMMEQKSTA VKALTGGIAH LFKQNKVVHV NGYGKITGKN QVTATKADGG TQVIDTKNIL 190 200 210 220 230 240 IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT 250 260 270 280 290 300 AVEFLGHVGG VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK 310 320 330 340 350 360 AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP 370 380 390 400 410 420 MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK 430 440 450 460 470 480 FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI 490 500 ARVCHAHPTL SEAFREANLA ASFGKSINF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases." Otulakowski G., Robinson B.H. J. Biol. Chem. 262:17313-17318(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-104.
[2]	"Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes." Pons G., Raefsky-Estrin C., Carothers D.J., Pepin R.A., Javed A.A., Jesse B.W., Ganapathi M.K., Samols D., Patel M.S. Proc. Natl. Acad. Sci. U.S.A. 85:1422-1426(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements." Feigenbaum A.S., Robinson B.H. Genomics 17:376-381(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-104. Tissue: Liver.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[9]	"Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene." Johanning G.L., Morris J.I., Madhusudhan K.T., Samols D., Patel M.S. Proc. Natl. Acad. Sci. U.S.A. 89:10964-10968(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143; LYS-410 AND LYS-417, MASS SPECTROMETRY.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations." Brautigam C.A., Chuang J.L., Tomchick D.R., Machius M., Chuang D.T. J. Mol. Biol. 350:543-552(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 36-509 IN COMPLEXES WITH NAD AND FAD, SUBUNIT.
[13]	"How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex." Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K., Korotchkina L.G., Patel M.S. J. Biol. Chem. 281:648-655(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 36-509.
[14]	"Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex." Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R., Chuang D.T. Structure 14:611-621(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 36-509 IN COMPLEX WITH PDHX, CHARACTERIZATION OF VARIANT DLD DEFICIENCY GLY-495.
[15]	"Identification of two missense mutations in a dihydrolipoamide dehydrogenase-deficient patient." Liu T.-C., Kim H., Arizmendi C., Kitano A., Patel M.S. Proc. Natl. Acad. Sci. U.S.A. 90:5186-5190(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DLD DEFICIENCY GLU-72 AND LEU-488.
[16]	"Identification of two mutations in a compound heterozygous child with dihydrolipoamide dehydrogenase deficiency." Hong Y.S., Kerr D.S., Craigen W.J., Tan J., Pan Y., Lusk M., Patel M.S. Hum. Mol. Genet. 5:1925-1930(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DLD DEFICIENCY GLY-495.
[17]	"Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews." Shaag A., Saada A., Berger I., Mandel H., Joseph A., Feigenbaum A., Elpeleg O.N. Am. J. Med. Genet. 82:177-182(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DLD DEFICIENCY CYS-229.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03490 mRNA. Translation: AAA59527.1.
J03620 mRNA. Translation: AAA35764.1.
L13761 , L13749, L13750, L13751, L13752, L13753, L13754, L13748, L13755, L13759, L13760, L13756, L13757, L13758 Genomic DNA. Translation: AAB01381.1.
AK312346 mRNA. Translation: BAG35267.1.
AB209703 mRNA. Translation: BAD92940.1. Different initiation.
CH236947 Genomic DNA. Translation: EAL24389.1.
CH471070 Genomic DNA. Translation: EAW83421.1.
BC018648 mRNA. Translation: AAH18648.1.
BC018696 mRNA. Translation: AAH18696.1.
M99384 Genomic DNA. Translation: AAA35759.1.

IPI

IPI00015911.

PIR

DEHULP. A92622.

RefSeq

NP_000099.2. NM_000108.3.

UniGene

Hs.131711.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZMC	X-ray	2.53	A/B/C/D/E/F/G/H	36-509	[»]
1ZMD	X-ray	2.08	A/B/C/D/E/F/G/H	36-509	[»]
1ZY8	X-ray	2.59	A/B/C/D/E/F/G/H/I/J	36-509	[»]
2F5Z	X-ray	2.18	A/B/C/D/E/F/G/H/I/J	36-509	[»]
3RNM	X-ray	2.40	A/B/C/D	36-509	[»]

ProteinModelPortal

P09622.

SMR

P09622. Positions 37-509.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29027N.

IntAct

P09622. 6 interactions.

MINT

MINT-3007138.

STRING

9606.ENSP00000205402.

PTM databases

PhosphoSite

P09622.

Polymorphism databases

DMDM

269849557.

2D gel databases

REPRODUCTION-2DPAGE

IPI00015911.

UCD-2DPAGE

P09622.

Proteomic databases

PaxDb

P09622.

PRIDE

P09622.

Protocols and materials databases

DNASU

1738.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000205402; ENSP00000205402; ENSG00000091140.
ENST00000417551; ENSP00000390667; ENSG00000091140.

GeneID

1738.

KEGG

hsa:1738.

UCSC

uc003vet.3. human.

Organism-specific databases

CTD

1738.

GeneCards

GC07P107531.

H-InvDB

HIX0006994.

HGNC

HGNC:2898. DLD.

HPA

HPA044849.

MIM

238331. gene.
248600. phenotype.

neXtProt

NX_P09622.

Orphanet

268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
255249. Leigh syndrome with nephrotic syndrome.
2394. Pyruvate dehydrogenase E3 deficiency.
268184. Thiamin-responsive maple syrup urine disease.

PharmGKB

PA27352.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1249.

HOGENOM

HOG000276708.

HOVERGEN

HBG002290.

InParanoid

P09622.

KO

K00382.

OMA

VANSRAK.

OrthoDB

EOG46Q6SC.

PhylomeDB

P09622.

Enzyme and pathway databases

BioCyc

MetaCyc:HS01727-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P09622.

Gene expression databases

ArrayExpress

P09622.

Bgee

P09622.

CleanEx

HS_DLD.

Genevestigator

P09622.

GermOnline

ENSG00000091140. Homo sapiens.

Family and domain databases

Gene3D

3.30.390.30. 1 hit.

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]

PANTHER

PTHR22912:SF20. PTHR22912:SF20. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

TIGRFAMs

TIGR01350. lipoamide_DH. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00157. NADH.

EvolutionaryTrace

P09622.

GenomeRNAi

1738.

NextBio

7047.

SOURCE

Search...

Entry information

Entry name

DLDH_HUMAN

Accession

Primary (citable) accession number: P09622
Secondary accession number(s): B2R5X0 , Q14131, Q14167, Q59EV8, Q8WTS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 24, 2009
Last modified:	May 29, 2013
This is version 170 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.