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Q92947

- GCDH_HUMAN

UniProt

Q92947 - GCDH_HUMAN

Protein

Glutaryl-CoA dehydrogenase, mitochondrial

Gene

GCDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    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.3 Publications

    Catalytic activityi

    Glutaryl-CoA + electron-transfer flavoprotein = crotonyl-CoA + CO2 + reduced electron-transfer flavoprotein.1 Publication

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei186 – 1861Substrate; via carbonyl oxygen
    Binding sitei319 – 3191FADBy similarity
    Binding sitei330 – 3301FADBy similarity
    Active sitei414 – 4141Proton acceptorCurated
    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 – 3915FADBy 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

    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

    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.
    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.
    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.
    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 – 4444MitochondrionSequence AnalysisAdd
    BLAST
    Chaini45 – 438394Glutaryl-CoA dehydrogenase, mitochondrialPRO_0000000526Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei240 – 2401N6-acetyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92947.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331G → A in AAC52079. (PubMed:1438360)Curated

    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.
    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.
    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.
    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. 1 PublicationVSP_000145Add
    BLAST

    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]
    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.

    Chemistry

    DrugBanki DB03147. Flavin adenine dinucleotide.

    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 ]
    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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 158 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