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Q60759 (GCDH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaryl-CoA dehydrogenase, mitochondrial

Short name=GCD
EC=1.3.8.6
Gene names
Name:Gcdh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

FAD.

Pathway

Amino-acid metabolism; lysine degradation.

Amino-acid metabolism; tryptophan metabolism.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Mitochondrion Potential
Chain45 – 438394Glutaryl-CoA dehydrogenase, mitochondrial
PRO_0000000528

Regions

Nucleotide binding177 – 18610FAD By similarity
Nucleotide binding177 – 1804FAD By similarity
Nucleotide binding212 – 2143FAD By similarity
Nucleotide binding387 – 3915FAD By similarity
Nucleotide binding416 – 4183FAD By similarity
Region138 – 1392Substrate binding By similarity
Region287 – 2948Substrate binding By similarity

Sites

Active site4141Proton acceptor By similarity
Binding site1861FAD By similarity
Binding site1861Substrate; via carbonyl oxygen By similarity
Binding site2941Substrate By similarity
Binding site3191FAD By similarity
Binding site3301FAD By similarity
Binding site4151Substrate; via amide nitrogen By similarity
Binding site4161FAD By similarity
Binding site4341FAD; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue511N6-acetyllysine; alternate Ref.6
Modified residue511N6-succinyllysine; alternate Ref.5
Modified residue651N6-acetyllysine Ref.6
Modified residue2401N6-acetyllysine Ref.6

Experimental info

Sequence conflict91R → Q in AAB04679. Ref.1
Sequence conflict751C → W in AAB04679. Ref.1
Sequence conflict821R → Q in AAB04679. Ref.1
Sequence conflict1671G → R in AAB04679. Ref.1
Sequence conflict2341R → P in AAB04679. Ref.1
Sequence conflict2451L → S in AAB04679. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60759 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A904457D76F2BD90

FASTA43848,606
        10         20         30         40         50         60 
MSLRGVSARL LSRRSGLRFP RFPRTWSSAA AHTEKTQIRP AKSSRPVFDW KDPLILEEQL 

        70         80         90        100        110        120 
TADEKLIRDT FRNYCQERLM SRILLANRNE VFHRDIVYEM GELGVLGPTI KGYGCAGVSS 

       130        140        150        160        170        180 
VAYGLLTREL ERVDSGYRSM MSVQSSLVMH PIYTYGSEEQ RQKYLPGLAK GELLGCFGLT 

       190        200        210        220        230        240 
EPNHGSDPGG METRARHNPS NQSYTLSGTK TWITNSPVAD LFIVWARCED NCIRGFILEK 

       250        260        270        280        290        300 
GMRGLSAPRI EGKFSLRASA TGMIIMDSVE VPEENVLPNV SSLAGPFGCL NTARYGITWG 

       310        320        330        340        350        360 
VLGAAEFCLH TARQYALDRI QFGVPLARNQ LVQKKLADML TEITLGLHAC LQLGRLKDQD 

       370        380        390        400        410        420 
KATPEMVSML KRNNCGKALD IARQARDILG GNGISDEYHV IRHAMNLEAV NTYEGTHDIH 

       430 
ALILGRAITG IQAFTVGK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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.
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18992 mRNA. Translation: AAB04679.1.
AK165406 mRNA. Translation: BAE38166.1.
BC061158 mRNA. Translation: AAH61158.1.
RefSeqNP_032123.3. NM_008097.2.
UniGeneMm.2475.

3D structure databases

ProteinModelPortalQ60759.
SMRQ60759. Positions 48-435.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid234755. 1 interaction.
IntActQ60759. 2 interactions.
MINTMINT-1861107.

PTM databases

PhosphoSiteQ60759.

Proteomic databases

PaxDbQ60759.
PRIDEQ60759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109745; ENSMUSP00000105367; ENSMUSG00000003809.
ENSMUST00000182458; ENSMUSP00000138554; ENSMUSG00000003809.
GeneID270076.
KEGGmmu:270076.
UCSCuc009mnx.1. mouse.

Organism-specific databases

CTD2639.
MGIMGI:104541. Gcdh.

Phylogenomic databases

eggNOGCOG1960.
GeneTreeENSGT00750000117480.
HOGENOMHOG000131662.
HOVERGENHBG001939.
InParanoidQ6P8N6.
KOK00252.
OMACYDTALR.
OrthoDBEOG7WT418.
TreeFamTF105051.

Enzyme and pathway databases

UniPathwayUPA00224.
UPA00225.

Gene expression databases

ArrayExpressQ60759.
BgeeQ60759.
CleanExMM_GCDH.
GenevestigatorQ60759.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. 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]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEPS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio393182.
PROQ60759.
SOURCESearch...

Entry information

Entry nameGCDH_MOUSE
AccessionPrimary (citable) accession number: Q60759
Secondary accession number(s): Q6P8N6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot