Reviewed, UniProtKB/Swiss-Prot Q8WZM4 (ETR2_CANTR)

Names and origin

Protein names

Recommended name:
    Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 2, mitochondrial
    EC=1.3.1.10
Alternative name(s):
    Trans-2-enoyl-CoA reductase 2
    EC=1.3.1.38

Gene names

Name:

ETR2

Organism

Candida tropicalis (Yeast)

Taxonomic identifier

5482 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	386 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	Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids. Ref.1
Catalytic activity	Acyl-[acyl-carrier-protein] + NADP+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.
Subunit structure	Homodimer and heterodimer with ETR1. Ref.1
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Inferred from electronic annotation. Source: EC trans-2-enoyl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 22

22

Mitochondrion Potential

Chain

23 – 386

364

Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 2, mitochondrial

PRO_0000000899

Secondary structure

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386

Helix Strand Turn

Details...

Beta strand

24 – 33

10

Helix

37 – 40

4

Beta strand

42 – 48

7

Beta strand

57 – 67

11

Helix

69 – 76

8

Beta strand

95 – 97

3

Beta strand

103 – 109

7

Beta strand

121 – 127

7

Beta strand

132 – 139

8

Helix

140 – 142

3

Beta strand

143 – 146

4

Helix

149 – 154

6

Helix

163 – 167

5

Beta strand

169 – 171

3

Helix

172 – 181

10

Turn

188 – 190

3

Beta strand

192 – 196

5

Helix

201 – 213

13

Beta strand

216 – 221

6

Helix

227 – 237

11

Beta strand

240 – 244

5

Helix

245 – 249

5

Helix

251 – 253

3

Helix

254 – 264

11

Beta strand

268 – 275

8

Helix

277 – 285

9

Beta strand

292 – 295

4

Beta strand

304 – 306

3

Helix

308 – 313

6

Beta strand

317 – 320

4

Helix

323 – 327

5

Helix

331 – 346

16

Beta strand

356 – 359

4

Beta strand

362 – 364

3

Helix

366 – 375

10

Helix

377 – 379

3

Beta strand

382 – 385

4

Sequences

	Sequence		Length	Mass (Da)
	Q8WZM4-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 91ABE00831F0C2E8	FASTA	386	42,117
	10 20 30 40 50 60 MYSVLKQSIR PRLLATHNQF RTMITAQAVL YTQHGEPKDV LFTQSFEIDD DNLAPNEVIV 70 80 90 100 110 120 KTLGSPINPS DINQIQGVYP SKPAKTTGFG TAEPAAPCGN EGLFEVIKVG SNVSSLEAGD 130 140 150 160 170 180 WVIPSHVNFG TWRTHALGND DDFIKLPNPA QSKANGKPNG LTINQGATIS VNPLTAYLML 190 200 210 220 230 240 THYVKLTPGK DWFIQNGGTS AVGKYASQIG KLLNFNSISV IRDRPNLDEV VASLKELGAT 250 260 270 280 290 300 QVITEDQNNS KEFGPTIKEW IKQSGGEAKL ALNCVGGKSS TGIARKLNNN GLMLTYGGMS 310 320 330 340 350 360 FQPVTIPTSL YIFKNFTSAG FWVTELLKNN KELKTSTLNQ IIAWYEEGKL TDAKSIETLY 370 380 DGTKPLHELY QDGVANSKDG KQLITY

References

[1]

"Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers." Torkko J.M., Koivuranta K.T., Kastaniotis A.J., Airenne T.T., Glumoff T., Ilves M., Hartig A., Gurvitz A., Hiltunen J.K. J. Biol. Chem. 278:41213-41220(2003) [PubMed: 12890667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT. Strain: ATCC 20336 / pK233 / NCYC 997.

[2]

"Crystal structure of enoyl thioester reductase 2." Airenne T.T., Torkko J.M., Hiltunen J.K. Submitted (JUN-2002) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

U94996 Genomic DNA. Translation: AAL55471.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H0K	X-ray	2.11	A/B	23-386	[»]
1N9G	X-ray	1.98	A/C/F	1-386	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.3.1.10. 1242.
1.3.1.38. 1242.

Family and domain databases

InterPro

IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR11695. ADH_Sf_Zn. 1 hit.

Pfam

PF08240. ADH_N. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ETR2_CANTR

Accession

Primary (citable) accession number: Q8WZM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)