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Protein

Probable trans-2-enoyl-CoA reductase, mitochondrial

Gene

CG16935

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis (By similarity).By similarity

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471NADPBy similarity
Binding sitei349 – 3491NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1764NADPBy similarity
Nucleotide bindingi196 – 1983NADPBy similarity
Nucleotide bindingi264 – 2674NADPBy similarity
Nucleotide bindingi289 – 2913NADPBy similarity

GO - Molecular functioni

  1. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Probable trans-2-enoyl-CoA reductase, mitochondrial (EC:1.3.1.38)
Gene namesi
ORF Names:CG16935
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033883. CG16935.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. microtubule associated complex Source: FlyBase
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionSequence AnalysisAdd
BLAST
Chaini20 – 357338Probable trans-2-enoyl-CoA reductase, mitochondrialPRO_0000000894Add
BLAST

Proteomic databases

PaxDbiQ9V6U9.

Expressioni

Gene expression databases

BgeeiQ9V6U9.
ExpressionAtlasiQ9V6U9. differential.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi62294. 2 interactions.
IntActiQ9V6U9. 2 interactions.
MINTiMINT-286445.

Structurei

3D structure databases

ProteinModelPortaliQ9V6U9.
SMRiQ9V6U9. Positions 17-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0604.
GeneTreeiENSGT00740000115589.
InParanoidiQ9V6U9.
KOiK07512.
OMAiCRAWGIN.
OrthoDBiEOG78M024.
PhylomeDBiQ9V6U9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9V6U9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRRGFLSRI NAAQWSRQMS VVAKSLKYTQ HGEPQEVLQL VEDKLPDPKD
60 70 80 90 100
NQVLVKILAA PINPADINTI QGKYPVKPKF PAVGGNECVA EVICVGDKVK
110 120 130 140 150
GFEAGQHVIP LASGLGTWTT HAVYKEDQLL IVSKKVGLAE AATSTVNPTT
160 170 180 190 200
AYRMLKDFVQ LCPGDTVIQN GANSAVGQAV HQLCRAWGIN SVGIVRDRPE
210 220 230 240 250
IAELKQMLQC LGATEVLTEA EIRTSDIFKS GKLKKPRLAF NCVGGKSATE
260 270 280 290 300
VSRHLDNGGV LVTYGGMSRE PVTVATGPLI FKDIAFRGFW MTRWSKENYS
310 320 330 340 350
SPERSKMFKE IFELMEQGKF VAPNHEMVPL AKFKDAAAAA LSFKGFTGKK

YILDMSI
Length:357
Mass (Da):39,111
Last modified:July 5, 2004 - v2
Checksum:i7E5F0D1EF9C70693
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58322.2.
RefSeqiNP_001286396.1. NM_001299467.1.
NP_610914.2. NM_137070.2.
UniGeneiDm.30974.

Genome annotation databases

EnsemblMetazoaiFBtr0087622; FBpp0086748; FBgn0033883.
GeneIDi36540.
KEGGidme:Dmel_CG16935.
UCSCiCG16935-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58322.2.
RefSeqiNP_001286396.1. NM_001299467.1.
NP_610914.2. NM_137070.2.
UniGeneiDm.30974.

3D structure databases

ProteinModelPortaliQ9V6U9.
SMRiQ9V6U9. Positions 17-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62294. 2 interactions.
IntActiQ9V6U9. 2 interactions.
MINTiMINT-286445.

Proteomic databases

PaxDbiQ9V6U9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087622; FBpp0086748; FBgn0033883.
GeneIDi36540.
KEGGidme:Dmel_CG16935.
UCSCiCG16935-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0033883. CG16935.

Phylogenomic databases

eggNOGiCOG0604.
GeneTreeiENSGT00740000115589.
InParanoidiQ9V6U9.
KOiK07512.
OMAiCRAWGIN.
OrthoDBiEOG78M024.
PhylomeDBiQ9V6U9.

Miscellaneous databases

GenomeRNAii36540.
NextBioi799088.
PROiQ9V6U9.

Gene expression databases

BgeeiQ9V6U9.
ExpressionAtlasiQ9V6U9. differential.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.

Entry informationi

Entry nameiMECR_DROME
AccessioniPrimary (citable) accession number: Q9V6U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: July 5, 2004
Last modified: January 7, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.