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Q92947 (GCDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Isoform Short is inactive. Ref.9 Ref.11

Catalytic activity

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

Cofactor

FAD.

Enzyme regulation

Strongly inhibited by MCPA-CoA, a metabolite of hypoglycin which is present in unripened fruit of the ackee tree. Ref.9

Pathway

Amino-acid metabolism; lysine degradation.

Amino-acid metabolism; tryptophan metabolism.

Subunit structure

Homotetramer. Ref.13 Ref.18

Subcellular location

Mitochondrion matrix.

Tissue specificity

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

Involvement in disease

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. Ref.2 Ref.3 Ref.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

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

KM=4.7 µM for glutaryl-CoA (at pH 6.5) Ref.9 Ref.11

KM=5.5 µM for glutaryl-CoA (at pH 7.5)

KM=8.1 µM for glutaryl-CoA (at pH 7.6)

KM=34.0 µM for glutaryl-CoA (at pH 8.5)

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q92947-1)

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.
Isoform Short (identifier: Q92947-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Mitochondrion Potential
Chain45 – 438394Glutaryl-CoA dehydrogenase, mitochondrial
PRO_0000000526

Regions

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

Sites

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

Amino acid modifications

Modified residue2401N6-acetyllysine By similarity

Natural variations

Alternative sequence415 – 43824GTHDI…FTASK → VVQMCSLKRRWNSL in isoform Short.
VSP_000145
Natural variant881R → C in GA1.
VAR_000366
Natural variant941R → L in GA1.
VAR_000367
Natural variant1011G → R in GA1. Ref.16
VAR_000368
Natural variant1151C → Y in GA1.
VAR_000369
Natural variant1221A → V in GA1.
VAR_000370
Natural variant1281R → G in GA1.
VAR_000371
Natural variant1381R → G in GA1; impaired protein stability and loss of activity. Ref.18
VAR_000372
Natural variant1391S → L in GA1.
VAR_000373
Natural variant1481V → I in GA1.
VAR_000374
Natural variant1611R → Q in GA1.
VAR_000375
Natural variant1781G → R in GA1.
VAR_000376
Natural variant1791L → R in GA1.
VAR_000377
Natural variant1911M → T in GA1.
VAR_000378
Natural variant1951A → T in GA1.
VAR_000379
Natural variant2271R → P in GA1.
VAR_000380
Natural variant2361F → L in GA1.
VAR_000381
Natural variant2571R → Q in GA1.
VAR_000382
Natural variant2571R → W in GA1.
VAR_000383
Natural variant2631M → V in GA1; severe phenotype despite a residual activity of 30% as measured in patient fibroblasts. Ref.17
VAR_060588
Natural variant2661M → V in GA1.
VAR_000384
Natural variant2781P → S in GA1.
VAR_000385
Natural variant2831L → P in GA1. Ref.16
VAR_000386
Natural variant2931A → T in GA1. Ref.16
VAR_000387
Natural variant2941R → W in GA1.
VAR_000388
Natural variant2951Y → H in GA1. Ref.2
VAR_000389
Natural variant2981A → T.
VAR_000390
Natural variant2981A → V.
VAR_000391
Natural variant3051S → L in GA1. Ref.16
VAR_000392
Natural variant3081C → S in GA1.
VAR_000393
Natural variant3091L → W in GA1.
VAR_000394
Natural variant3131R → W in GA1.
VAR_000395
Natural variant3331Q → E in GA1.
VAR_000396
Natural variant3491A → T in GA1.
VAR_000397
Natural variant3541G → R in GA1.
VAR_000398
Natural variant3541G → S in GA1.
VAR_000399
Natural variant3551R → C in GA1.
VAR_000400
Natural variant3551R → H in GA1.
VAR_000401
Natural variant3651E → K in GA1.
VAR_000402
Natural variant3751C → R in GA1.
VAR_000403
Natural variant3821A → T in GA1.
VAR_000404
Natural variant3831R → C in GA1.
VAR_000405
Natural variant3831R → H in GA1.
VAR_000406
Natural variant3861R → Q in GA1.
VAR_000407
Natural variant3901G → A in GA1.
VAR_000409
Natural variant3901G → R in GA1. Ref.16
VAR_000408
Natural variant3921N → D in GA1.
VAR_000410
Natural variant4001V → M in GA1.
VAR_000411
Natural variant4021R → Q in GA1.
VAR_000413
Natural variant4021R → W in GA1; most common mutation identified; loss of tetramerization and enzyme activity. Ref.18
VAR_000412
Natural variant4031H → R in GA1.
VAR_000414
Natural variant4061N → K in GA1.
VAR_000415
Natural variant4071L → P in GA1.
VAR_000416
Natural variant4141E → K in GA1; loss of enzyme activity. Ref.18
VAR_000417
Natural variant4161T → I in GA1. Ref.16
VAR_000418
Natural variant4211A → T in GA1.
Corresponds to variant rs151201155 [ dbSNP | Ensembl ].
VAR_000419
Natural variant4211A → V in GA1; impaired association of subunits.
VAR_000420
Natural variant4291T → M in GA1.
VAR_000421
Natural variant4331A → E in GA1.
VAR_000422

Experimental info

Mutagenesis4141E → D: Reduced catalytic activity.
Sequence conflict331G → A in AAC52079. Ref.1

Secondary structure

....................................................... 438
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 415B8D510027BB63

FASTA43848,127
        10         20         30         40         50         60 
MALRGVSVRL LSRGPGLHVL RTWVSSAAQT EKGGRTQSQL AKSSRPEFDW QDPLVLEEQL 

        70         80         90        100        110        120 
TTDEILIRDT FRTYCQERLM PRILLANRNE VFHREIISEM GELGVLGPTI KGYGCAGVSS 

       130        140        150        160        170        180 
VAYGLLAREL ERVDSGYRSA MSVQSSLVMH PIYAYGSEEQ RQKYLPQLAK GELLGCFGLT 

       190        200        210        220        230        240 
EPNSGSDPSS METRAHYNSS NKSYTLNGTK TWITNSPMAD LFVVWARCED GCIRGFLLEK 

       250        260        270        280        290        300 
GMRGLSAPRI QGKFSLRASA TGMIIMDGVE VPEENVLPGA SSLGGPFGCL NNARYGIAWG 

       310        320        330        340        350        360 
VLGASEFCLH TARQYALDRM QFGVPLARNQ LIQKKLADML TEITLGLHAC LQLGRLKDQD 

       370        380        390        400        410        420 
KAAPEMVSLL KRNNCGKALD IARQARDMLG GNGISDEYHV IRHAMNLEAV NTYEGTHDIH 

       430 
ALILGRAITG IQAFTASK 

« Hide

Isoform Short [UniParc].

Checksum: 8E9E298E6DA9433C
Show »

FASTA42847,355

References

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

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U69141 mRNA. Translation: AAB08455.1.
AF012342 expand/collapse EMBL AC list , 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.
PIRT44260.
T45073.
RefSeqNP_000150.1. NM_000159.3.
NP_039663.1. NM_013976.3.
UniGeneHs.532699.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SIQX-ray2.10A47-438[»]
1SIRX-ray2.60A45-438[»]
2R0MX-ray2.70A45-438[»]
2R0NX-ray2.30A45-438[»]
ProteinModelPortalQ92947.
SMRQ92947. Positions 47-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108909. 15 interactions.
IntActQ92947. 11 interactions.
STRING9606.ENSP00000222214.

PTM databases

PhosphoSiteQ92947.

Polymorphism databases

DMDM2492631.

Proteomic databases

PaxDbQ92947.
PRIDEQ92947.

Protocols and materials databases

DNASU2639.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222214; ENSP00000222214; ENSG00000105607. [Q92947-1]
ENST00000457854; ENSP00000394872; ENSG00000105607. [Q92947-2]
ENST00000591470; ENSP00000466845; ENSG00000105607. [Q92947-1]
GeneID2639.
KEGGhsa:2639.
UCSCuc002mvp.4. human. [Q92947-2]
uc002mvq.4. human. [Q92947-1]

Organism-specific databases

CTD2639.
GeneCardsGC19P013001.
HGNCHGNC:4189. GCDH.
HPAHPA043252.
HPA048492.
MIM231670. phenotype.
608801. gene.
neXtProtNX_Q92947.
Orphanet25. Glutaryl-CoA dehydrogenase deficiency.
PharmGKBPA28604.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1960.
HOGENOMHOG000131662.
HOVERGENHBG001939.
InParanoidQ92947.
KOK00252.
OMACYDTALR.
PhylomeDBQ92947.
TreeFamTF105051.

Enzyme and pathway databases

BRENDA1.3.99.7. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ92947.
UniPathwayUPA00224.
UPA00225.

Gene expression databases

ArrayExpressQ92947.
BgeeQ92947.
CleanExHS_GCDH.
GenevestigatorQ92947.

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.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGCDH. human.
EvolutionaryTraceQ92947.
GenomeRNAi2639.
NextBio10404.
PROQ92947.
SOURCESearch...

Entry information

Entry nameGCDH_HUMAN
AccessionPrimary (citable) accession number: Q92947
Secondary accession number(s): A8K2Z2, O14719
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM