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Q9V6U9

- MECR_DROME

UniProt

Q9V6U9 - MECR_DROME

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Protein
Probable trans-2-enoyl-CoA reductase, mitochondrial
Gene
CG16935
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1764NADP By similarity
Nucleotide bindingi196 – 1983NADP By similarity
Nucleotide bindingi264 – 2674NADP By similarity
Nucleotide bindingi289 – 2913NADP By 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 – 1919Mitochondrion Reviewed prediction
Add
BLAST
Chaini20 – 357338Probable trans-2-enoyl-CoA reductase, mitochondrial
PRO_0000000894Add
BLAST

Proteomic databases

PaxDbiQ9V6U9.

Expressioni

Gene expression databases

BgeeiQ9V6U9.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi62294. 2 interactions.
MINTiMINT-286445.

Structurei

3D structure databases

ProteinModelPortaliQ9V6U9.
SMRiQ9V6U9. Positions 17-355.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0604.
GeneTreeiENSGT00740000115589.
InParanoidiQ9V6U9.
KOiK07512.
OMAiCSTLWRV.
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

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MLRRGFLSRI NAAQWSRQMS VVAKSLKYTQ HGEPQEVLQL VEDKLPDPKD    50
NQVLVKILAA PINPADINTI QGKYPVKPKF PAVGGNECVA EVICVGDKVK 100
GFEAGQHVIP LASGLGTWTT HAVYKEDQLL IVSKKVGLAE AATSTVNPTT 150
AYRMLKDFVQ LCPGDTVIQN GANSAVGQAV HQLCRAWGIN SVGIVRDRPE 200
IAELKQMLQC LGATEVLTEA EIRTSDIFKS GKLKKPRLAF NCVGGKSATE 250
VSRHLDNGGV LVTYGGMSRE PVTVATGPLI FKDIAFRGFW MTRWSKENYS 300
SPERSKMFKE IFELMEQGKF VAPNHEMVPL AKFKDAAAAA LSFKGFTGKK 350
YILDMSI 357
Length:357
Mass (Da):39,111
Last modified:July 5, 2004 - v2
Checksum:i7E5F0D1EF9C70693
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF58322.2.
RefSeqiNP_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:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF58322.2 .
RefSeqi NP_610914.2. NM_137070.2.
UniGenei Dm.30974.

3D structure databases

ProteinModelPortali Q9V6U9.
SMRi Q9V6U9. Positions 17-355.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62294. 2 interactions.
MINTi MINT-286445.

Proteomic databases

PaxDbi Q9V6U9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0087622 ; FBpp0086748 ; FBgn0033883 .
GeneIDi 36540.
KEGGi dme:Dmel_CG16935.
UCSCi CG16935-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0033883. CG16935.

Phylogenomic databases

eggNOGi COG0604.
GeneTreei ENSGT00740000115589.
InParanoidi Q9V6U9.
KOi K07512.
OMAi CSTLWRV.
OrthoDBi EOG78M024.
PhylomeDBi Q9V6U9.

Miscellaneous databases

GenomeRNAii 36540.
NextBioi 799088.
PROi Q9V6U9.

Gene expression databases

Bgeei Q9V6U9.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 93 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

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