Reviewed, UniProtKB/Swiss-Prot Q5EU90 (TER_EUGGR)

Names and origin

Protein names

Recommended name:
    Trans-2-enoyl-CoA reductase, mitochondrial
    EC=1.3.1.44

Gene names

Name:

TER

Organism

Euglena gracilis

Taxonomic identifier

3039 [NCBI]

Taxonomic lineage

Eukaryota › Euglenozoa › Euglenida › Euglenales › Euglena

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes reduction of enoyl-CoA to acyl-CoA, an important step of fatty acid biosynthesis which is performed under anaerobiosis. Under anaeobiosis, mitochondria perform a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. Can use both NADH and NADPH as electron donor, with 2-3-fold higher specific activities for NADH relative to NADPH.
Catalytic activity	Acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH. Ref.1
Subunit structure	Monomer.
Subcellular location	Mitochondrion Ref.1.
Developmental stage	Expressed under aerobic and anaerobic conditions. Ref.1
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the TER reductase family.
Biophysicochemical properties	Kinetic parameters: KM=68 µM for NADH KM=119 µM for NADPH KM=91 µM for trans-2-hexenoyl-CoA

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	trans-2-enoyl-CoA reductase (NAD+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 68	68	Mitochondrion By similarity
	Chain	69 – 539	471	Trans-2-enoyl-CoA reductase, mitochondrial		PRO_0000033619

Sequences

	Sequence		Length	Mass (Da)
	Q5EU90-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: A52C244AC61E2CDF	FASTA	539	57,303
	10 20 30 40 50 60 MSCPASPSAA VVSAGALCLC VATVLLATGS NPTALSTAST RSPTSLVRGV DRGLMRPTTA 70 80 90 100 110 120 AALTTMREVP QMAEGFSGEA TSAWAAAGPQ WAAPLVAAAS SALALWWWAA RRSVRRPLAA 130 140 150 160 170 180 LAELPTAVTH LAPPMAMFTT TAKVIQPKIR GFICTTTHPI GCEKRVQEEI AYARAHPPTS 190 200 210 220 230 240 PGPKRVLVIG CSTGYGLSTR ITAAFGYQAA TLGVFLAGPP TKGRPAAAGW YNTVAFEKAA 250 260 270 280 290 300 LEAGLYARSL NGDAFDSTTK ARTVEAIKRD LGTVDLVVYS IAAPKRTDPA TGVLHKACLK 310 320 330 340 350 360 PIGATYTNRT VNTDKAEVTD VSIEPASPEE IADTVKVMGG EDWELWIQAL SEAGVLAEGA 370 380 390 400 410 420 KTVAYSYIGP EMTWPVYWSG TIGEAKKDVE KAAKRITQQY GCPAYPVVAK ALVTQASSAI 430 440 450 460 470 480 PVVPLYICLL YRVMKEKGTH EGCIEQMVRL LTTKLYPENG APIVDEAGRV RVDDWEMAED 490 500 510 520 530 VQQAVKDLWS QVSTANLKDI SDFAGYQTEF LRLFGFGIDG VDYDQPVDVE ADLPSAAQQ

References

[1]

"Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis." Hoffmeister M., Piotrowski M., Nowitzki U., Martin W. J. Biol. Chem. 280:4329-4338(2005) [PubMed: 15569691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BLOCKAGE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY, ENZYME ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE. Strain: SAG 1224-5/25.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY741582 mRNA. Translation: AAW66853.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.3.1.44. 260.
Family and domain databases
InterPro	IPR010758. Uncharacterised_TER_reductase. [Graphical view]
Pfam	PF07055. scADH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TER_EUGGR

Accession

Primary (citable) accession number: Q5EU90

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	March 15, 2005
Last modified:	November 24, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)