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UniProtKB/Swiss-Prot entry Q8LCU7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MECR_ARATH
Primary accession number Q8LCU7
Secondary accession numbers Q8W4H6 Q9M166
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 40)
Name and origin of the protein
Protein name Probable trans-2-enoyl-CoA reductase, mitochondrial [Precursor]
Synonym EC 1.3.1.38
Gene name
OrderedLocusNames: At3g45770
ORFNames: T6D9.100
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL157735; CAB75790.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY062554; AAL32632.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY114655; AAM47974.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086398; AAM64465.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T47517; T47517.
RefSeq NP_566881.1; -.
UniGene At.3719
3D structure databases
HSSP Q8WZM4; 1H0K. [HSSP ENTRY / PDB]
ModBase Q8LCU7.
Organism-specific databases
GeneFarm 2939; -.
TAIR At3g45770; -.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from direct assay from TAIR).
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from direct assay from TAIR).
GO:0005524; Molecular function: ATP binding (inferred from direct assay from TAIR).
GO:0019166; Molecular function: trans-2-enoyl-CoA reductase (NADPH) activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
Proteomics databases
PRIDE Q8LCU7; -.
Genome annotation databases
GeneID 823720; -.
GenomeReviews BA000014_GR; AT3G45770.
KEGG ath:AT3G45770; -.
Other
ProtoNet Q8LCU7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; Oxidoreductase; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    27  27     Mitochondrion (Potential). 
CHAIN   28   375  348     Probable trans-2-enoyl-CoA reductase, mitochondrial. PRO_0000000895
CONFLICT   293   293        K -> E (in Ref. 2; AAL32632/AAM47974). 
Sequence information
Length: 375 AA [This is the length of the unprocessed precursor] Molecular weight: 40823 Da [This is the MW of the unprocessed precursor] CRC64: 9047BCD122872F48 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAALMESVVG RALKFSSTAN FRSIRRGETP TLCIKSFSTI MSPPSKAIVY EEHGSPDSVT 

        70         80         90        100        110        120 
RLVNLPPVEV KENDVCVKMI AAPINPSDIN RIEGVYPVRP PVPAVGGYEG VGEVYAVGSN 

       130        140        150        160        170        180 
VNGFSPGDWV IPSPPSSGTW QTYVVKEESV WHKIDKECPM EYAATITVNP LTALRMLEDF 

       190        200        210        220        230        240 
VNLNSGDSVV QNGATSIVGQ CVIQLARLRG ISTINLIRDR AGSDEAREQL KALGADEVFS 

       250        260        270        280        290        300 
ESQLNVKNVK SLLGNLPEPA LGFNCVGGNA ASLVLKYLRE GGTMVTYGGM SKKPITVSTT 

       310        320        330        340        350        360 
SFIFKDLALR GFWLQSWLSM GKVKECREMI DYLLGLARDG KLKYETELVP FEEFPVALDK 

       370 
ALGKLGRQPK QVITF 

Q8LCU7 in FASTA format

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