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P11310

- ACADM_HUMAN

UniProt

P11310 - ACADM_HUMAN

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Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADM

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

Functioni

This enzyme is specific for acyl chain lengths of 4 to 16.

Catalytic activityi

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FAD1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671Substrate; via carbonyl oxygen
Binding sitei216 – 2161Substrate
Active sitei401 – 4011Proton acceptor
Binding sitei402 – 4021Substrate; via amide nitrogen
Binding sitei413 – 4131Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FAD1 Publication
Nucleotide bindingi191 – 1933FAD1 Publication
Nucleotide bindingi306 – 3083FAD1 Publication
Nucleotide bindingi316 – 3172FAD1 Publication
Nucleotide bindingi374 – 3785FAD1 Publication
Nucleotide bindingi403 – 4053FAD1 Publication

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: InterPro
  3. identical protein binding Source: BHF-UCL
  4. medium-chain-acyl-CoA dehydrogenase activity Source: BHF-UCL

GO - Biological processi

  1. cardiac muscle cell differentiation Source: Ensembl
  2. carnitine biosynthetic process Source: BHF-UCL
  3. carnitine metabolic process, CoA-linked Source: BHF-UCL
  4. cellular lipid metabolic process Source: Reactome
  5. fatty acid beta-oxidation Source: UniProtKB
  6. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: BHF-UCL
  7. glycogen biosynthetic process Source: Ensembl
  8. liver development Source: Ensembl
  9. medium-chain fatty acid catabolic process Source: BHF-UCL
  10. medium-chain fatty acid metabolic process Source: BHF-UCL
  11. oxidation-reduction process Source: BHF-UCL
  12. post-embryonic development Source: Ensembl
  13. regulation of gluconeogenesis Source: Ensembl
  14. response to cold Source: Ensembl
  15. response to starvation Source: Ensembl
  16. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS04089-MONOMER.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
SABIO-RKP11310.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
Gene namesi
Name:ACADM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:89. ACADM.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: LIFEdb
  5. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) [MIM:201450]: An inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy.14 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531R → C in ACADMD.
VAR_000317
Natural varianti67 – 671Y → H in ACADMD; mild. 1 Publication
VAR_013698
Natural varianti78 – 781I → T in ACADMD. 1 Publication
VAR_015954
Natural varianti115 – 1162Missing in ACADMD. 1 Publication
VAR_000318
Natural varianti116 – 1161C → Y in ACADMD. 1 Publication
VAR_015955
Natural varianti121 – 1211T → I in ACADMD. 1 Publication
VAR_015956
Natural varianti149 – 1491M → I in ACADMD. 1 Publication
VAR_000319
Natural varianti193 – 1931T → A in ACADMD; the thermostability is markedly decreased. 1 Publication
VAR_000320
Natural varianti195 – 1951G → R in ACADMD. 1 Publication
VAR_000321
Natural varianti206 – 2061R → L in ACADMD. 1 Publication
VAR_015957
Natural varianti244 – 2441C → R in ACADMD. 1 Publication
VAR_000322
Natural varianti245 – 2451S → L in ACADMD. 1 Publication
VAR_013699
Natural varianti267 – 2671G → R in ACADMD. 1 Publication
VAR_000323
Natural varianti281 – 2811R → T in ACADMD; mild or benign clinical phenotype. 1 Publication
VAR_013700
Natural varianti310 – 3101G → R in ACADMD. 1 Publication
VAR_015958
Natural varianti326 – 3261M → T in ACADMD. 1 Publication
VAR_000324
Natural varianti329 – 3291K → E in ACADMD; most common variant. 6 Publications
Corresponds to variant rs77931234 [ dbSNP | Ensembl ].
VAR_000325
Natural varianti336 – 3361S → R in ACADMD. 1 Publication
VAR_000326
Natural varianti352 – 3521Y → C in ACADMD. 1 Publication
VAR_015959
Natural varianti375 – 3751I → T in ACADMD. 1 Publication
VAR_000327

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861L → M: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi98 – 981L → W: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi100 – 1001L → Y: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi108 – 1081I → M: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi191 – 1911W → A: Loss of electron transfer to ETF. 1 Publication
Mutagenesisi191 – 1911W → F: Reduces rate of electron transfer to ETF about six-fold. 1 Publication
Mutagenesisi237 – 2371E → A: Strongly reduced rate of electron transfer to ETF. 2 Publications
Mutagenesisi384 – 3841E → A: Reduces rate of electron transfer to ETF three-fold. 2 Publications
Mutagenesisi384 – 3841E → Q: Reduces rate of electron transfer to ETF two-fold. 2 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi201450. phenotype.
Orphaneti42. Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKBiPA24425.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionAdd
BLAST
Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691N6-acetyllysine; alternateBy similarity
Modified residuei69 – 691N6-succinyllysine; alternateBy similarity
Modified residuei179 – 1791N6-succinyllysineBy similarity
Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity
Modified residuei217 – 2171N6-acetyllysine; alternateBy similarity
Modified residuei217 – 2171N6-succinyllysine; alternateBy similarity
Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
Modified residuei271 – 2711N6-acetyllysine; alternateBy similarity
Modified residuei271 – 2711N6-succinyllysine; alternateBy similarity
Modified residuei279 – 2791N6-acetyllysine1 Publication
Modified residuei301 – 3011N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity (By similarity). These sites are deacetylated by SIRT3.By similarity1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP11310.
PaxDbiP11310.
PRIDEiP11310.

2D gel databases

REPRODUCTION-2DPAGEIPI00005040.
UCD-2DPAGEP11310.

PTM databases

PhosphoSiteiP11310.

Expressioni

Gene expression databases

BgeeiP11310.
CleanExiHS_ACADM.
ExpressionAtlasiP11310. baseline and differential.
GenevestigatoriP11310.

Organism-specific databases

HPAiHPA006198.
HPA026542.

Interactioni

Subunit structurei

Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF.3 Publications

Protein-protein interaction databases

BioGridi106552. 13 interactions.
DIPiDIP-34281N.
IntActiP11310. 7 interactions.
MINTiMINT-3007693.
STRINGi9606.ENSP00000409612.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Helixi43 – 5917Combined sources
Helixi61 – 7010Combined sources
Helixi75 – 8410Combined sources
Helixi93 – 953Combined sources
Helixi102 – 11514Combined sources
Helixi117 – 12913Combined sources
Helixi131 – 1366Combined sources
Helixi139 – 15113Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi165 – 1684Combined sources
Helixi169 – 1713Combined sources
Beta strandi175 – 1784Combined sources
Beta strandi180 – 19314Combined sources
Turni194 – 1974Combined sources
Beta strandi199 – 2068Combined sources
Helixi215 – 2173Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi247 – 25812Combined sources
Helixi259 – 2613Combined sources
Beta strandi262 – 2654Combined sources
Turni266 – 2683Combined sources
Helixi269 – 30335Combined sources
Beta strandi309 – 3124Combined sources
Helixi313 – 3153Combined sources
Helixi317 – 34529Combined sources
Helixi351 – 37626Combined sources
Helixi377 – 3793Combined sources
Helixi387 – 3948Combined sources
Helixi395 – 3984Combined sources
Turni399 – 4013Combined sources
Helixi404 – 41714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGCX-ray2.60A/B/C/D26-421[»]
1EGDX-ray2.40A/B/C/D26-421[»]
1EGEX-ray2.75A/B/C/D26-421[»]
1T9GX-ray2.90A/B/C/D26-421[»]
2A1TX-ray2.80A/B/C/D1-421[»]
ProteinModelPortaliP11310.
SMRiP11310. Positions 35-421.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11310.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Substrate binding

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP11310.
KOiK00249.
OrthoDBiEOG74FF0S.
PhylomeDBiP11310.
TreeFamiTF105020.

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 1 (identifier: P11310-1) [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

        10         20         30         40         50
MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA
60 70 80 90 100
TARKFAREEI IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL
110 120 130 140 150
GTFDACLISE ELAYGCTGVQ TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT
160 170 180 190 200
EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW
210 220 230 240 250
YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM GQRCSDTRGI
260 270 280 290 300
VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT
310 320 330 340 350
KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN
360 370 380 390 400
TYYASIAKAF AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY
410 420
EGTSQIQRLI VAREHIDKYK N
Length:421
Mass (Da):46,588
Last modified:July 1, 1989 - v1
Checksum:i7CD0B5832410581B
GO
Isoform 2 (identifier: P11310-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: R → RCSLQ

Show »
Length:425
Mass (Da):47,020
Checksum:iC6A133404E1B6E70
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561I → T in AAF63626. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531R → C in ACADMD.
VAR_000317
Natural varianti67 – 671Y → H in ACADMD; mild. 1 Publication
VAR_013698
Natural varianti78 – 781I → T in ACADMD. 1 Publication
VAR_015954
Natural varianti115 – 1162Missing in ACADMD. 1 Publication
VAR_000318
Natural varianti116 – 1161C → Y in ACADMD. 1 Publication
VAR_015955
Natural varianti121 – 1211T → I in ACADMD. 1 Publication
VAR_015956
Natural varianti132 – 1321P → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035716
Natural varianti149 – 1491M → I in ACADMD. 1 Publication
VAR_000319
Natural varianti193 – 1931T → A in ACADMD; the thermostability is markedly decreased. 1 Publication
VAR_000320
Natural varianti195 – 1951G → R in ACADMD. 1 Publication
VAR_000321
Natural varianti206 – 2061R → L in ACADMD. 1 Publication
VAR_015957
Natural varianti244 – 2441C → R in ACADMD. 1 Publication
VAR_000322
Natural varianti245 – 2451S → L in ACADMD. 1 Publication
VAR_013699
Natural varianti267 – 2671G → R in ACADMD. 1 Publication
VAR_000323
Natural varianti281 – 2811R → T in ACADMD; mild or benign clinical phenotype. 1 Publication
VAR_013700
Natural varianti310 – 3101G → R in ACADMD. 1 Publication
VAR_015958
Natural varianti326 – 3261M → T in ACADMD. 1 Publication
VAR_000324
Natural varianti329 – 3291K → E in ACADMD; most common variant. 6 Publications
Corresponds to variant rs77931234 [ dbSNP | Ensembl ].
VAR_000325
Natural varianti336 – 3361S → R in ACADMD. 1 Publication
VAR_000326
Natural varianti352 – 3521Y → C in ACADMD. 1 Publication
VAR_015959
Natural varianti375 – 3751I → T in ACADMD. 1 Publication
VAR_000327

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei10 – 101R → RCSLQ in isoform 2. 1 PublicationVSP_038420

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16827 mRNA. Translation: AAA51566.1.
M91432
, M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, M91431 Genomic DNA. Translation: AAA59567.1.
AF251043 mRNA. Translation: AAF63626.1.
AK312629 mRNA. Translation: BAG35514.1.
AL357314 Genomic DNA. Translation: CAI22390.1.
CH471059 Genomic DNA. Translation: EAX06401.1.
BC005377 mRNA. Translation: AAH05377.1.
M60505 Genomic DNA. Translation: AAB59625.1.
CCDSiCCDS44165.1. [P11310-2]
CCDS668.1. [P11310-1]
PIRiA29031. DEHUCM.
RefSeqiNP_000007.1. NM_000016.5. [P11310-1]
NP_001120800.1. NM_001127328.2. [P11310-2]
UniGeneiHs.445040.

Genome annotation databases

EnsembliENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
GeneIDi34.
KEGGihsa:34.
UCSCiuc001dgw.4. human. [P11310-1]
uc009wbp.3. human. [P11310-2]

Polymorphism databases

DMDMi113017.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16827 mRNA. Translation: AAA51566.1 .
M91432
, M91421 , M91422 , M91423 , M91425 , M91426 , M91427 , M91428 , M91429 , M91430 , M91431 Genomic DNA. Translation: AAA59567.1 .
AF251043 mRNA. Translation: AAF63626.1 .
AK312629 mRNA. Translation: BAG35514.1 .
AL357314 Genomic DNA. Translation: CAI22390.1 .
CH471059 Genomic DNA. Translation: EAX06401.1 .
BC005377 mRNA. Translation: AAH05377.1 .
M60505 Genomic DNA. Translation: AAB59625.1 .
CCDSi CCDS44165.1. [P11310-2 ]
CCDS668.1. [P11310-1 ]
PIRi A29031. DEHUCM.
RefSeqi NP_000007.1. NM_000016.5. [P11310-1 ]
NP_001120800.1. NM_001127328.2. [P11310-2 ]
UniGenei Hs.445040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EGC X-ray 2.60 A/B/C/D 26-421 [» ]
1EGD X-ray 2.40 A/B/C/D 26-421 [» ]
1EGE X-ray 2.75 A/B/C/D 26-421 [» ]
1T9G X-ray 2.90 A/B/C/D 26-421 [» ]
2A1T X-ray 2.80 A/B/C/D 1-421 [» ]
ProteinModelPortali P11310.
SMRi P11310. Positions 35-421.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106552. 13 interactions.
DIPi DIP-34281N.
IntActi P11310. 7 interactions.
MINTi MINT-3007693.
STRINGi 9606.ENSP00000409612.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSitei P11310.

Polymorphism databases

DMDMi 113017.

2D gel databases

REPRODUCTION-2DPAGE IPI00005040.
UCD-2DPAGE P11310.

Proteomic databases

MaxQBi P11310.
PaxDbi P11310.
PRIDEi P11310.

Protocols and materials databases

DNASUi 34.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370841 ; ENSP00000359878 ; ENSG00000117054 . [P11310-1 ]
ENST00000420607 ; ENSP00000409612 ; ENSG00000117054 . [P11310-2 ]
GeneIDi 34.
KEGGi hsa:34.
UCSCi uc001dgw.4. human. [P11310-1 ]
uc009wbp.3. human. [P11310-2 ]

Organism-specific databases

CTDi 34.
GeneCardsi GC01P076190.
GeneReviewsi ACADM.
HGNCi HGNC:89. ACADM.
HPAi HPA006198.
HPA026542.
MIMi 201450. phenotype.
607008. gene.
neXtProti NX_P11310.
Orphaneti 42. Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKBi PA24425.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00760000119007.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
InParanoidi P11310.
KOi K00249.
OrthoDBi EOG74FF0S.
PhylomeDBi P11310.
TreeFami TF105020.

Enzyme and pathway databases

UniPathwayi UPA00660 .
BioCyci MetaCyc:HS04089-MONOMER.
Reactomei REACT_116145. PPARA activates gene expression.
REACT_160. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
REACT_1697. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
REACT_1708. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
SABIO-RK P11310.

Miscellaneous databases

EvolutionaryTracei P11310.
GenomeRNAii 34.
NextBioi 131.
PROi P11310.
SOURCEi Search...

Gene expression databases

Bgeei P11310.
CleanExi HS_ACADM.
ExpressionAtlasi P11310. baseline and differential.
Genevestigatori P11310.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue."
    Kelly D.P., Kim J.-J.P., Billadello J.J., Hainline B.E., Chu T.W., Strauss A.W.
    Proc. Natl. Acad. Sci. U.S.A. 84:4068-4072(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene."
    Zhang Z.F., Kelly D.P., Kim J.-J.P., Zhou Y.Q., Ogden M.L., Whelan A.J., Strauss A.W.
    Biochemistry 31:81-89(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  3. "Medium-chain acyl-CoA dehydrogenase."
    Sun F., Wang Y., Block G.D.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Colon.
  4. "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 1).
    Tissue: Heart.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 1).
    Tissue: Liver.
  8. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 218-235, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  9. "Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency."
    Matsubara Y., Narisawa K., Miyabayashi S., Tada K., Coates P.M., Bachmann C., Elsas L.J. II, Pollitt R.J., Rhead W.J., Roe C.R.
    Biochem. Biophys. Res. Commun. 171:498-505(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342, VARIANT ACADMD GLU-329.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279 AND LYS-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating conserved lysines near the active site."
    Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M., Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E., Gibson B.W., Hirschey M.D., Goetzman E.S.
    J. Biol. Chem. 288:33837-33847(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEACETYLATION BY SIRT3.
  13. "Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity."
    Lee H.J., Wang M., Paschke R., Nandy A., Ghisla S., Kim J.-J.P.
    Biochemistry 35:12412-12420(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND THE SUBSTRATE ANALOG OCTANOYL-COENZYME A, COFACTOR, SUBUNIT.
  14. "Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain acyl-CoA dehydrogenase complex."
    Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S., Leys D.
    J. Biol. Chem. 279:32904-32912(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-421 IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF LEU-86; LEU-98; LEU-100; ILE-108; GLU-237 AND GLU-384, SUBUNIT.
  15. "Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein."
    Toogood H.S., van Thiel A., Scrutton N.S., Leys D.
    J. Biol. Chem. 280:30361-30366(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF TRP-191; GLU-237 AND GLU-384, SUBUNIT.
  16. Cited for: REVIEW ON VARIANTS ACADMD.
  17. "Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation."
    Yokota I., Indo Y., Coates P.M., Tanaka K.
    J. Clin. Invest. 86:1000-1003(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACADMD GLU-329.
  18. "Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency."
    Kelly D.P., Whelan A.J., Ogden M.L., Alpers R., Zhang Z.F., Bellus G., Gregersen N., Dorland L., Strauss A.W.
    Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACADMD GLU-329.
  19. "Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency."
    Yokota I., Coates P.M., Hale D.E., Rinaldo P., Tanaka K.
    Am. J. Hum. Genet. 49:1280-1291(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADMD ILE-149; ARG-244; ARG-267 AND THR-375.
  20. "Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli."
    Gregersen N., Andresen B.S., Bross P., Winter V., Ruediger N., Engst S., Christensen E., Kelly D., Strauss A.W., Koelvraa S., Bolund L., Ghisla S.
    Hum. Genet. 86:545-551(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACADMD GLU-329.
  21. "Frequency of the G985 MCAD mutation in the general population."
    Blakemore A.I., Singleton H., Pollitt R.J., Engel P.C., Kolvraa S., Gregersen N., Curtis D.
    Lancet 337:298-299(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACADMD GLU-329 FREQUENCY.
  22. "Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene."
    Andresen B.S., Jensen T.G., Bross P., Knudsen I., Winter V., Koelvraa S., Bolund L., Ding J.-H., Chen Y.-T., van Hove J.L.K., Curtis D., Yokota I., Tanaka K., Kim J.-J.P., Gregersen N.
    Am. J. Hum. Genet. 54:975-988(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADMD THR-326 AND ARG-336.
  23. "Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies."
    Ziadeh R., Hoffman E.P., Finegold D.N., Hoop R.C., Brackett J.C., Strauss A.W., Naylor E.W.
    Pediatr. Res. 37:675-678(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACADMD 115-GLY-CYS-116 DEL.
  24. "A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death."
    Brackett J.C., Sims H.F., Steiner R.D., Nunge M., Zimmerman E.M., Demartinville B., Rinaldo P., Slaugh R., Strauss A.W.
    J. Clin. Invest. 94:1477-1483(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACADMD ARG-195.
  25. "The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype?"
    Andresen B.S., Bross P., Udvari S., Kirk J., Gray G., Kmoch S., Chamoles N., Knudsen I., Winter V., Wilcken B., Yokota I., Hart K., Packman S., Harpey J.P., Saudubray J.-M., Hale D.E., Bolund L., Koelvraa S., Gregersen N.
    Hum. Mol. Genet. 6:695-707(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352.
  26. "Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site."
    Kuchler B., Abdel-Ghany A.G., Bross P., Nandy A., Rasched I., Ghisla S.
    Biochem. J. 337:225-230(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT ACADMD ALA-193.
  27. "Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency."
    Yang B.-Z., Ding J.-H., Zhou C., Dimachkie M.M., Sweetman L., Dasouki M.J., Wilkinson J., Roe C.R.
    Mol. Genet. Metab. 69:259-262(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADMD LEU-206 AND GLU-329.
  28. "Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency."
    Andresen B.S., Dobrowolski S.F., O'Reilly L., Muenzer J., McCandless S.E., Frazier D.M., Udvari S., Bross P., Knudsen I., Banas R., Chace D.H., Engel P.C., Naylor E.W., Gregersen N.
    Am. J. Hum. Genet. 68:1408-1418(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADMD HIS-67; THR-78; ILE-121 AND ARG-310.
  29. Cited for: VARIANT ACADMD LEU-245.
  30. "Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency."
    Albers S., Levy H.L., Irons M., Strauss A.W., Marsden D.
    J. Inherit. Metab. Dis. 24:417-418(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACADMD THR-281 AND GLU-329.
  31. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-132.

Entry informationi

Entry nameiACADM_HUMAN
AccessioniPrimary (citable) accession number: P11310
Secondary accession number(s): Q5T4U4, Q9NYF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 178 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

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.
Utilizes the electron transfer flavoprotein (ETF) as electron acceptor that transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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