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Protein

Glutaryl-CoA dehydrogenase, mitochondrial

Gene

Gcdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

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

Cofactori

Pathwayi: lysine degradation

This protein is involved in the pathway lysine degradation, which is part of Amino-acid metabolism.
View all proteins of this organism that are known to be involved in the pathway lysine degradation and in Amino-acid metabolism.

Pathwayi: tryptophan metabolism

This protein is involved in the pathway tryptophan metabolism, which is part of Amino-acid metabolism.
View all proteins of this organism that are known to be involved in the pathway tryptophan metabolism and in Amino-acid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861FADBy similarity
Binding sitei186 – 1861Substrate; via carbonyl oxygenBy similarity
Binding sitei294 – 2941SubstrateBy similarity
Binding sitei319 – 3191FADBy similarity
Binding sitei330 – 3301FADBy similarity
Active sitei414 – 4141Proton acceptorBy similarity
Binding sitei415 – 4151Substrate; via amide nitrogenBy similarity
Binding sitei416 – 4161FADBy similarity
Binding sitei434 – 4341FAD; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 18610FADBy similarity
Nucleotide bindingi177 – 1804FADBy similarity
Nucleotide bindingi212 – 2143FADBy similarity
Nucleotide bindingi387 – 3915FADBy similarity
Nucleotide bindingi416 – 4183FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-6133-MONOMER.
BRENDAi1.3.8.6. 3474.
ReactomeiR-MMU-71064. Lysine catabolism.
UniPathwayiUPA00224.
UPA00225.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaryl-CoA dehydrogenase, mitochondrial (EC:1.3.8.6)
Short name:
GCD
Gene namesi
Name:Gcdh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:104541. Gcdh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Animals show highly increased protein glutarylation in liver.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4444MitochondrionSequence analysisAdd
BLAST
Chaini45 – 438394Glutaryl-CoA dehydrogenase, mitochondrialPRO_0000000528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine; alternateCombined sources
Modified residuei51 – 511N6-succinyllysine; alternateCombined sources
Modified residuei65 – 651N6-acetyllysineCombined sources
Modified residuei240 – 2401N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ60759.
MaxQBiQ60759.
PaxDbiQ60759.
PRIDEiQ60759.

PTM databases

iPTMnetiQ60759.
PhosphoSiteiQ60759.

Expressioni

Gene expression databases

BgeeiQ60759.
CleanExiMM_GCDH.
ExpressionAtlasiQ60759. baseline and differential.
GenevisibleiQ60759. MM.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi234755. 1 interaction.
IntActiQ60759. 2 interactions.
MINTiMINT-1861107.
STRINGi10090.ENSMUSP00000003907.

Structurei

3D structure databases

ProteinModelPortaliQ60759.
SMRiQ60759. Positions 48-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0138. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131662.
HOVERGENiHBG001939.
InParanoidiQ60759.
KOiK00252.
OrthoDBiEOG7WT418.
TreeFamiTF105051.

Family and domain databases

Gene3Di1.10.540.10. 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.
PROSITEiPS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q60759-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLRGVSARL LSRRSGLRFP RFPRTWSSAA AHTEKTQIRP AKSSRPVFDW
60 70 80 90 100
KDPLILEEQL TADEKLIRDT FRNYCQERLM SRILLANRNE VFHRDIVYEM
110 120 130 140 150
GELGVLGPTI KGYGCAGVSS VAYGLLTREL ERVDSGYRSM MSVQSSLVMH
160 170 180 190 200
PIYTYGSEEQ RQKYLPGLAK GELLGCFGLT EPNHGSDPGG METRARHNPS
210 220 230 240 250
NQSYTLSGTK TWITNSPVAD LFIVWARCED NCIRGFILEK GMRGLSAPRI
260 270 280 290 300
EGKFSLRASA TGMIIMDSVE VPEENVLPNV SSLAGPFGCL NTARYGITWG
310 320 330 340 350
VLGAAEFCLH TARQYALDRI QFGVPLARNQ LVQKKLADML TEITLGLHAC
360 370 380 390 400
LQLGRLKDQD KATPEMVSML KRNNCGKALD IARQARDILG GNGISDEYHV
410 420 430
IRHAMNLEAV NTYEGTHDIH ALILGRAITG IQAFTVGK
Length:438
Mass (Da):48,606
Last modified:July 27, 2011 - v2
Checksum:iA904457D76F2BD90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91R → Q in AAB04679 (PubMed:7490088).Curated
Sequence conflicti75 – 751C → W in AAB04679 (PubMed:7490088).Curated
Sequence conflicti82 – 821R → Q in AAB04679 (PubMed:7490088).Curated
Sequence conflicti167 – 1671G → R in AAB04679 (PubMed:7490088).Curated
Sequence conflicti234 – 2341R → P in AAB04679 (PubMed:7490088).Curated
Sequence conflicti245 – 2451L → S in AAB04679 (PubMed:7490088).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18992 mRNA. Translation: AAB04679.1.
AK165406 mRNA. Translation: BAE38166.1.
BC061158 mRNA. Translation: AAH61158.1.
RefSeqiNP_032123.3. NM_008097.2.
UniGeneiMm.2475.

Genome annotation databases

EnsembliENSMUST00000109745; ENSMUSP00000105367; ENSMUSG00000003809.
GeneIDi270076.
KEGGimmu:270076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18992 mRNA. Translation: AAB04679.1.
AK165406 mRNA. Translation: BAE38166.1.
BC061158 mRNA. Translation: AAH61158.1.
RefSeqiNP_032123.3. NM_008097.2.
UniGeneiMm.2475.

3D structure databases

ProteinModelPortaliQ60759.
SMRiQ60759. Positions 48-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234755. 1 interaction.
IntActiQ60759. 2 interactions.
MINTiMINT-1861107.
STRINGi10090.ENSMUSP00000003907.

PTM databases

iPTMnetiQ60759.
PhosphoSiteiQ60759.

Proteomic databases

EPDiQ60759.
MaxQBiQ60759.
PaxDbiQ60759.
PRIDEiQ60759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109745; ENSMUSP00000105367; ENSMUSG00000003809.
GeneIDi270076.
KEGGimmu:270076.

Organism-specific databases

CTDi2639.
MGIiMGI:104541. Gcdh.

Phylogenomic databases

eggNOGiKOG0138. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131662.
HOVERGENiHBG001939.
InParanoidiQ60759.
KOiK00252.
OrthoDBiEOG7WT418.
TreeFamiTF105051.

Enzyme and pathway databases

UniPathwayiUPA00224.
UPA00225.
BioCyciRETL1328306-WGS:GSTH-6133-MONOMER.
BRENDAi1.3.8.6. 3474.
ReactomeiR-MMU-71064. Lysine catabolism.

Miscellaneous databases

PROiQ60759.
SOURCEiSearch...

Gene expression databases

BgeeiQ60759.
CleanExiMM_GCDH.
ExpressionAtlasiQ60759. baseline and differential.
GenevisibleiQ60759. MM.

Family and domain databases

Gene3Di1.10.540.10. 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.
PROSITEiPS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, structure, and chromosome localization of the mouse glutaryl-CoA dehydrogenase gene."
    Koeller D.M., Digiulio K.A., Angeloni S.V., Dowler L.L., Frerman F.E., White R.A., Goodman S.I.
    Genomics 28:508-512(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Sv.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "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: Kidney.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-65 AND LYS-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiGCDH_MOUSE
AccessioniPrimary (citable) accession number: Q60759
Secondary accession number(s): Q6P8N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.