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Q92947

- GCDH_HUMAN

UniProt

Q92947 - GCDH_HUMAN

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Protein

Glutaryl-CoA dehydrogenase, mitochondrial

Gene
GCDH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO2 in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive.2 Publications

Catalytic activityi

Glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein.

Cofactori

FAD.

Enzyme regulationi

Strongly inhibited by MCPA-CoA, a metabolite of hypoglycin which is present in unripened fruit of the ackee tree.1 Publication

Kineticsi

Release of crotonyl-CoA product from the enzyme is the rate-determining step in its steady-state turnover.

  1. KM=4.7 µM for glutaryl-CoA (at pH 6.5)2 Publications
  2. KM=5.5 µM for glutaryl-CoA (at pH 7.5)
  3. KM=8.1 µM for glutaryl-CoA (at pH 7.6)
  4. KM=34.0 µM for glutaryl-CoA (at pH 8.5)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861Substrate; via carbonyl oxygen
Binding sitei319 – 3191FAD By similarity
Binding sitei330 – 3301FAD By similarity
Active sitei414 – 4141Proton acceptor Inferred
Binding sitei415 – 4151Substrate; via amide nitrogen
Binding sitei434 – 4341FAD; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 18610FAD
Nucleotide bindingi212 – 2143FAD
Nucleotide bindingi387 – 3915FAD By similarity
Nucleotide bindingi416 – 4183FAD

GO - Molecular functioni

  1. fatty-acyl-CoA binding Source: Ensembl
  2. flavin adenine dinucleotide binding Source: Ensembl
  3. glutaryl-CoA dehydrogenase activity Source: Reactome

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. fatty acid oxidation Source: Ensembl
  3. fatty-acyl-CoA biosynthetic process Source: Ensembl
  4. lysine catabolic process Source: Reactome
  5. small molecule metabolic process Source: Reactome
  6. tryptophan metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.3.99.7. 2681.
ReactomeiREACT_1298. Lysine catabolism.
SABIO-RKQ92947.
UniPathwayiUPA00224.
UPA00225.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaryl-CoA dehydrogenase, mitochondrial (EC:1.3.8.6)
Short name:
GCD
Gene namesi
Name:GCDH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:4189. GCDH.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Ensembl
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Glutaric aciduria 1 (GA1) [MIM:231670]: An autosomal recessive metabolic disorder characterized by progressive dystonia and athetosis due to gliosis and neuronal loss in the basal ganglia.
Note: The disease is caused by mutations affecting the gene represented in this entry.6 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881R → C in GA1.
VAR_000366
Natural varianti94 – 941R → L in GA1.
VAR_000367
Natural varianti101 – 1011G → R in GA1. 1 Publication
VAR_000368
Natural varianti115 – 1151C → Y in GA1.
VAR_000369
Natural varianti122 – 1221A → V in GA1.
VAR_000370
Natural varianti128 – 1281R → G in GA1.
VAR_000371
Natural varianti138 – 1381R → G in GA1; impaired protein stability and loss of activity. 1 Publication
VAR_000372
Natural varianti139 – 1391S → L in GA1.
VAR_000373
Natural varianti148 – 1481V → I in GA1.
VAR_000374
Natural varianti161 – 1611R → Q in GA1.
VAR_000375
Natural varianti178 – 1781G → R in GA1.
VAR_000376
Natural varianti179 – 1791L → R in GA1.
VAR_000377
Natural varianti191 – 1911M → T in GA1.
VAR_000378
Natural varianti195 – 1951A → T in GA1.
VAR_000379
Natural varianti227 – 2271R → P in GA1.
VAR_000380
Natural varianti236 – 2361F → L in GA1.
VAR_000381
Natural varianti257 – 2571R → Q in GA1.
VAR_000382
Natural varianti257 – 2571R → W in GA1.
VAR_000383
Natural varianti263 – 2631M → V in GA1; severe phenotype despite a residual activity of 30% as measured in patient fibroblasts. 1 Publication
VAR_060588
Natural varianti266 – 2661M → V in GA1.
VAR_000384
Natural varianti278 – 2781P → S in GA1.
VAR_000385
Natural varianti283 – 2831L → P in GA1. 1 Publication
VAR_000386
Natural varianti293 – 2931A → T in GA1. 1 Publication
VAR_000387
Natural varianti294 – 2941R → W in GA1.
VAR_000388
Natural varianti295 – 2951Y → H in GA1. 1 Publication
VAR_000389
Natural varianti305 – 3051S → L in GA1. 1 Publication
VAR_000392
Natural varianti308 – 3081C → S in GA1.
VAR_000393
Natural varianti309 – 3091L → W in GA1.
VAR_000394
Natural varianti313 – 3131R → W in GA1.
VAR_000395
Natural varianti333 – 3331Q → E in GA1.
VAR_000396
Natural varianti349 – 3491A → T in GA1.
VAR_000397
Natural varianti354 – 3541G → R in GA1.
VAR_000398
Natural varianti354 – 3541G → S in GA1.
VAR_000399
Natural varianti355 – 3551R → C in GA1.
VAR_000400
Natural varianti355 – 3551R → H in GA1.
VAR_000401
Natural varianti365 – 3651E → K in GA1.
VAR_000402
Natural varianti375 – 3751C → R in GA1.
VAR_000403
Natural varianti382 – 3821A → T in GA1.
VAR_000404
Natural varianti383 – 3831R → C in GA1.
VAR_000405
Natural varianti383 – 3831R → H in GA1.
VAR_000406
Natural varianti386 – 3861R → Q in GA1.
VAR_000407
Natural varianti390 – 3901G → A in GA1.
VAR_000409
Natural varianti390 – 3901G → R in GA1. 1 Publication
VAR_000408
Natural varianti392 – 3921N → D in GA1.
VAR_000410
Natural varianti400 – 4001V → M in GA1.
VAR_000411
Natural varianti402 – 4021R → Q in GA1.
VAR_000413
Natural varianti402 – 4021R → W in GA1; most common mutation identified; loss of tetramerization and enzyme activity. 1 Publication
VAR_000412
Natural varianti403 – 4031H → R in GA1.
VAR_000414
Natural varianti406 – 4061N → K in GA1.
VAR_000415
Natural varianti407 – 4071L → P in GA1.
VAR_000416
Natural varianti414 – 4141E → K in GA1; loss of enzyme activity. 1 Publication
VAR_000417
Natural varianti416 – 4161T → I in GA1. 1 Publication
VAR_000418
Natural varianti421 – 4211A → T in GA1.
Corresponds to variant rs151201155 [ dbSNP | Ensembl ].
VAR_000419
Natural varianti421 – 4211A → V in GA1; impaired association of subunits.
VAR_000420
Natural varianti429 – 4291T → M in GA1.
VAR_000421
Natural varianti433 – 4331A → E in GA1.
VAR_000422

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi414 – 4141E → D: Reduced catalytic activity.

Keywords - Diseasei

Disease mutation, Glutaricaciduria

Organism-specific databases

MIMi231670. phenotype.
Orphaneti25. Glutaryl-CoA dehydrogenase deficiency.
PharmGKBiPA28604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4444Mitochondrion Reviewed predictionAdd
BLAST
Chaini45 – 438394Glutaryl-CoA dehydrogenase, mitochondrialPRO_0000000526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei240 – 2401N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ92947.
PaxDbiQ92947.
PRIDEiQ92947.

PTM databases

PhosphoSiteiQ92947.

Expressioni

Tissue specificityi

Isoform 1 and isoform 2 are expressed in fibroblasts and liver.

Gene expression databases

ArrayExpressiQ92947.
BgeeiQ92947.
CleanExiHS_GCDH.
GenevestigatoriQ92947.

Organism-specific databases

HPAiHPA043252.
HPA048492.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRB2P629931EBI-1236978,EBI-401755
NOS3P294741EBI-1236978,EBI-1391623
PSEN1P497681EBI-1236978,EBI-297277

Protein-protein interaction databases

BioGridi108909. 15 interactions.
IntActiQ92947. 11 interactions.
STRINGi9606.ENSP00000222214.

Structurei

Secondary structure

1
438
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 594
Helixi62 – 7817
Helixi80 – 8910
Helixi95 – 1028
Helixi120 – 13112
Helixi135 – 14612
Helixi149 – 1557
Helixi158 – 16912
Beta strandi175 – 1784
Beta strandi184 – 1863
Helixi188 – 1903
Beta strandi194 – 1985
Turni199 – 2024
Beta strandi203 – 21412
Helixi216 – 2183
Beta strandi220 – 2289
Beta strandi233 – 2397
Beta strandi254 – 2563
Beta strandi261 – 27212
Helixi273 – 2753
Helixi284 – 31835
Helixi326 – 3283
Helixi330 – 35829
Helixi364 – 38825
Helixi389 – 3946
Helixi396 – 3983
Helixi400 – 41011
Beta strandi413 – 4153
Helixi417 – 42913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SIQX-ray2.10A47-438[»]
1SIRX-ray2.60A45-438[»]
2R0MX-ray2.70A45-438[»]
2R0NX-ray2.30A45-438[»]
ProteinModelPortaliQ92947.
SMRiQ92947. Positions 47-436.

Miscellaneous databases

EvolutionaryTraceiQ92947.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 1392Substrate binding
Regioni287 – 2948Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
HOGENOMiHOG000131662.
HOVERGENiHBG001939.
InParanoidiQ92947.
KOiK00252.
OMAiAYRDEHY.
PhylomeDBiQ92947.
TreeFamiTF105051.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q92947-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MALRGVSVRL LSRGPGLHVL RTWVSSAAQT EKGGRTQSQL AKSSRPEFDW    50
QDPLVLEEQL TTDEILIRDT FRTYCQERLM PRILLANRNE VFHREIISEM 100
GELGVLGPTI KGYGCAGVSS VAYGLLAREL ERVDSGYRSA MSVQSSLVMH 150
PIYAYGSEEQ RQKYLPQLAK GELLGCFGLT EPNSGSDPSS METRAHYNSS 200
NKSYTLNGTK TWITNSPMAD LFVVWARCED GCIRGFLLEK GMRGLSAPRI 250
QGKFSLRASA TGMIIMDGVE VPEENVLPGA SSLGGPFGCL NNARYGIAWG 300
VLGASEFCLH TARQYALDRM QFGVPLARNQ LIQKKLADML TEITLGLHAC 350
LQLGRLKDQD KAAPEMVSLL KRNNCGKALD IARQARDMLG GNGISDEYHV 400
IRHAMNLEAV NTYEGTHDIH ALILGRAITG IQAFTASK 438
Length:438
Mass (Da):48,127
Last modified:February 1, 1997 - v1
Checksum:i415B8D510027BB63
GO
Isoform Short (identifier: Q92947-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     415-438: GTHDIHALILGRAITGIQAFTASK → VVQMCSLKRRWNSL

Show »
Length:428
Mass (Da):47,355
Checksum:i8E9E298E6DA9433C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881R → C in GA1.
VAR_000366
Natural varianti94 – 941R → L in GA1.
VAR_000367
Natural varianti101 – 1011G → R in GA1. 1 Publication
VAR_000368
Natural varianti115 – 1151C → Y in GA1.
VAR_000369
Natural varianti122 – 1221A → V in GA1.
VAR_000370
Natural varianti128 – 1281R → G in GA1.
VAR_000371
Natural varianti138 – 1381R → G in GA1; impaired protein stability and loss of activity. 1 Publication
VAR_000372
Natural varianti139 – 1391S → L in GA1.
VAR_000373
Natural varianti148 – 1481V → I in GA1.
VAR_000374
Natural varianti161 – 1611R → Q in GA1.
VAR_000375
Natural varianti178 – 1781G → R in GA1.
VAR_000376
Natural varianti179 – 1791L → R in GA1.
VAR_000377
Natural varianti191 – 1911M → T in GA1.
VAR_000378
Natural varianti195 – 1951A → T in GA1.
VAR_000379
Natural varianti227 – 2271R → P in GA1.
VAR_000380
Natural varianti236 – 2361F → L in GA1.
VAR_000381
Natural varianti257 – 2571R → Q in GA1.
VAR_000382
Natural varianti257 – 2571R → W in GA1.
VAR_000383
Natural varianti263 – 2631M → V in GA1; severe phenotype despite a residual activity of 30% as measured in patient fibroblasts. 1 Publication
VAR_060588
Natural varianti266 – 2661M → V in GA1.
VAR_000384
Natural varianti278 – 2781P → S in GA1.
VAR_000385
Natural varianti283 – 2831L → P in GA1. 1 Publication
VAR_000386
Natural varianti293 – 2931A → T in GA1. 1 Publication
VAR_000387
Natural varianti294 – 2941R → W in GA1.
VAR_000388
Natural varianti295 – 2951Y → H in GA1. 1 Publication
VAR_000389
Natural varianti298 – 2981A → T.
VAR_000390
Natural varianti298 – 2981A → V.
VAR_000391
Natural varianti305 – 3051S → L in GA1. 1 Publication
VAR_000392
Natural varianti308 – 3081C → S in GA1.
VAR_000393
Natural varianti309 – 3091L → W in GA1.
VAR_000394
Natural varianti313 – 3131R → W in GA1.
VAR_000395
Natural varianti333 – 3331Q → E in GA1.
VAR_000396
Natural varianti349 – 3491A → T in GA1.
VAR_000397
Natural varianti354 – 3541G → R in GA1.
VAR_000398
Natural varianti354 – 3541G → S in GA1.
VAR_000399
Natural varianti355 – 3551R → C in GA1.
VAR_000400
Natural varianti355 – 3551R → H in GA1.
VAR_000401
Natural varianti365 – 3651E → K in GA1.
VAR_000402
Natural varianti375 – 3751C → R in GA1.
VAR_000403
Natural varianti382 – 3821A → T in GA1.
VAR_000404
Natural varianti383 – 3831R → C in GA1.
VAR_000405
Natural varianti383 – 3831R → H in GA1.
VAR_000406
Natural varianti386 – 3861R → Q in GA1.
VAR_000407
Natural varianti390 – 3901G → A in GA1.
VAR_000409
Natural varianti390 – 3901G → R in GA1. 1 Publication
VAR_000408
Natural varianti392 – 3921N → D in GA1.
VAR_000410
Natural varianti400 – 4001V → M in GA1.
VAR_000411
Natural varianti402 – 4021R → Q in GA1.
VAR_000413
Natural varianti402 – 4021R → W in GA1; most common mutation identified; loss of tetramerization and enzyme activity. 1 Publication
VAR_000412
Natural varianti403 – 4031H → R in GA1.
VAR_000414
Natural varianti406 – 4061N → K in GA1.
VAR_000415
Natural varianti407 – 4071L → P in GA1.
VAR_000416
Natural varianti414 – 4141E → K in GA1; loss of enzyme activity. 1 Publication
VAR_000417
Natural varianti416 – 4161T → I in GA1. 1 Publication
VAR_000418
Natural varianti421 – 4211A → T in GA1.
Corresponds to variant rs151201155 [ dbSNP | Ensembl ].
VAR_000419
Natural varianti421 – 4211A → V in GA1; impaired association of subunits.
VAR_000420
Natural varianti429 – 4291T → M in GA1.
VAR_000421
Natural varianti433 – 4331A → E in GA1.
VAR_000422

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei415 – 43824GTHDI…FTASK → VVQMCSLKRRWNSL in isoform Short. VSP_000145Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331G → A in AAC52079. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69141 mRNA. Translation: AAB08455.1.
AF012342
, AF012339, AF012340, AF012341 Genomic DNA. Translation: AAC52079.1.
BT006706 mRNA. Translation: AAP35352.1.
AK290407 mRNA. Translation: BAF83096.1.
AD000092 Genomic DNA. Translation: AAB51174.1.
CH471106 Genomic DNA. Translation: EAW84324.1.
BC002579 mRNA. Translation: AAH02579.1.
CCDSiCCDS12286.1. [Q92947-1]
PIRiT44260.
T45073.
RefSeqiNP_000150.1. NM_000159.3. [Q92947-1]
NP_039663.1. NM_013976.3. [Q92947-2]
UniGeneiHs.532699.

Genome annotation databases

EnsembliENST00000222214; ENSP00000222214; ENSG00000105607. [Q92947-1]
ENST00000457854; ENSP00000394872; ENSG00000105607. [Q92947-2]
ENST00000591470; ENSP00000466845; ENSG00000105607. [Q92947-1]
GeneIDi2639.
KEGGihsa:2639.
UCSCiuc002mvp.4. human. [Q92947-2]
uc002mvq.4. human. [Q92947-1]

Polymorphism databases

DMDMi2492631.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69141 mRNA. Translation: AAB08455.1 .
AF012342
, AF012339 , AF012340 , AF012341 Genomic DNA. Translation: AAC52079.1 .
BT006706 mRNA. Translation: AAP35352.1 .
AK290407 mRNA. Translation: BAF83096.1 .
AD000092 Genomic DNA. Translation: AAB51174.1 .
CH471106 Genomic DNA. Translation: EAW84324.1 .
BC002579 mRNA. Translation: AAH02579.1 .
CCDSi CCDS12286.1. [Q92947-1 ]
PIRi T44260.
T45073.
RefSeqi NP_000150.1. NM_000159.3. [Q92947-1 ]
NP_039663.1. NM_013976.3. [Q92947-2 ]
UniGenei Hs.532699.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SIQ X-ray 2.10 A 47-438 [» ]
1SIR X-ray 2.60 A 45-438 [» ]
2R0M X-ray 2.70 A 45-438 [» ]
2R0N X-ray 2.30 A 45-438 [» ]
ProteinModelPortali Q92947.
SMRi Q92947. Positions 47-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108909. 15 interactions.
IntActi Q92947. 11 interactions.
STRINGi 9606.ENSP00000222214.

PTM databases

PhosphoSitei Q92947.

Polymorphism databases

DMDMi 2492631.

Proteomic databases

MaxQBi Q92947.
PaxDbi Q92947.
PRIDEi Q92947.

Protocols and materials databases

DNASUi 2639.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222214 ; ENSP00000222214 ; ENSG00000105607 . [Q92947-1 ]
ENST00000457854 ; ENSP00000394872 ; ENSG00000105607 . [Q92947-2 ]
ENST00000591470 ; ENSP00000466845 ; ENSG00000105607 . [Q92947-1 ]
GeneIDi 2639.
KEGGi hsa:2639.
UCSCi uc002mvp.4. human. [Q92947-2 ]
uc002mvq.4. human. [Q92947-1 ]

Organism-specific databases

CTDi 2639.
GeneCardsi GC19P013001.
HGNCi HGNC:4189. GCDH.
HPAi HPA043252.
HPA048492.
MIMi 231670. phenotype.
608801. gene.
neXtProti NX_Q92947.
Orphaneti 25. Glutaryl-CoA dehydrogenase deficiency.
PharmGKBi PA28604.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
HOGENOMi HOG000131662.
HOVERGENi HBG001939.
InParanoidi Q92947.
KOi K00252.
OMAi AYRDEHY.
PhylomeDBi Q92947.
TreeFami TF105051.

Enzyme and pathway databases

UniPathwayi UPA00224 .
UPA00225 .
BRENDAi 1.3.99.7. 2681.
Reactomei REACT_1298. Lysine catabolism.
SABIO-RK Q92947.

Miscellaneous databases

ChiTaRSi GCDH. human.
EvolutionaryTracei Q92947.
GenomeRNAii 2639.
NextBioi 10404.
PROi Q92947.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92947.
Bgeei Q92947.
CleanExi HS_GCDH.
Genevestigatori Q92947.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
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Publicationsi

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  1. "Pork and human cDNAs encoding glutaryl-CoA dehydrogenase."
    Goodman S.I., Kratz L.E., Frerman F.E.
    Prog. Clin. Biol. Res. 375:169-173(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Tissue: Liver.
  2. "Cloning of glutaryl-CoA dehydrogenase cDNA, and expression of wild type and mutant enzymes in Escherichia coli."
    Goodman S.I., Kratz L.E., Digiulio K.A., Biery B.J., Goodman K.E., Isaya G., Frerman F.E.
    Hum. Mol. Genet. 4:1493-1498(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), FUNCTION, CATALYTIC ACTIVITY, VARIANT GA1 HIS-295.
    Tissue: Liver.
  3. "The human glutaryl-CoA dehydrogenase gene: report of intronic sequences and of 13 novel mutations causing glutaric aciduria type I."
    Schwartz M., Christensen E., Superti-Furga A., Brandt N.J.
    Hum. Genet. 102:452-458(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GA1.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
  5. "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] (ISOFORM LONG).
    Tissue: Umbilical cord blood.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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] (ISOFORM LONG).
    Tissue: Lymph.
  9. "Specific glutaryl-CoA dehydrogenating activity is deficient in cultured fibroblasts from glutaric aciduria patients."
    Hyman D.B., Tanaka K.
    J. Clin. Invest. 73:778-784(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Glutaryl-CoA dehydrogenase mutations in glutaric acidemia (type I): review and report of thirty novel mutations."
    Goodman S.I., Stein D.E., Schlesinger S., Christensen E., Schwartz M., Greenberg C.R., Elpeleg O.N.
    Hum. Mutat. 12:141-144(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  11. "Kinetic mechanism of glutaryl-CoA dehydrogenase."
    Rao K.S., Albro M., Dwyer T.M., Frerman F.E.
    Biochemistry 45:15853-15861(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions."
    Fu Z., Wang M., Paschke R., Rao K.S., Frerman F.E., Kim J.-J.P.
    Biochemistry 43:9674-9684(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 47-438 IN COMPLEXES WITH SUBSTRATE ANALOG AND FAD, SUBUNIT.
  14. "The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate."
    Rao K.S., Fu Z., Albro M., Narayanan B., Baddam S., Lee H.-J.K., Kim J.-J.P., Frerman F.E.
    Biochemistry 46:14468-14477(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 45-438 OF MUTANT ASP-414 IN COMPLEXES WITH SUBSTRATE AND FAD.
  15. "Gene structure and mutations of glutaryl-coenzyme A dehydrogenase: impaired association of enzyme subunits that is due to an A421V substitution causes glutaric acidemia type I in the Amish."
    Biery B.J., Stein D.E., Morton D.H., Goodman S.I.
    Am. J. Hum. Genet. 59:1006-1011(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GA1.
  16. "Glutaric aciduria type I in the Arab and Jewish communities in Israel."
    Anikster Y., Shaag A., Joseph A., Mandel H., Ben-Zeev B., Christensen E., Elpeleg O.N.
    Am. J. Hum. Genet. 59:1012-1018(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GA1 ARG-101; PRO-283; THR-293; LEU-305; ARG-390 AND ILE-416.
  17. "Severe phenotype despite high residual glutaryl-CoA dehydrogenase activity: a novel mutation in a Turkish patient with glutaric aciduria type I."
    Muehlhausen C., Christensen E., Schwartz M., Muschol N., Ullrich K., Lukacs Z.
    J. Inherit. Metab. Dis. 26:713-714(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GA1 VAL-263.
  18. "Disease-causing missense mutations affect enzymatic activity, stability and oligomerization of glutaryl-CoA dehydrogenase (GCDH)."
    Keyser B., Muehlhausen C., Dickmanns A., Christensen E., Muschol N., Ullrich K., Braulke T.
    Hum. Mol. Genet. 17:3854-3863(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS GA1 GLY-138; TRP-402 AND LYS-414, SUBUNIT.

Entry informationi

Entry nameiGCDH_HUMAN
AccessioniPrimary (citable) accession number: Q92947
Secondary accession number(s): A8K2Z2, O14719
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: September 3, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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