[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-29, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. STRAIN=ATCC 20336 / pK233 / NCYC 997; DOI=10.1128/MCB.21.18.6243-6253.2001; PubMed=11509667 [NCBI, ExPASy, EBI, Israel, Japan] Torkko J.M., Koivuranta K.T., Miinalainen I.J., Yagi A.I., Schmitz W., Kastaniotis A.J., Airenne T.T., Gurvitz A., Hiltunen K.J.; "Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence."; Mol. Cell. Biol. 21:6243-6253(2001).
[2]	SUBUNIT. STRAIN=ATCC 20336 / pK233 / NCYC 997; DOI=10.1074/jbc.M307664200; PubMed=12890667 [NCBI, ExPASy, EBI, Israel, Japan] Torkko J.M., Koivuranta K.T., Kastaniotis A.J., Airenne T.T., Glumoff T., Ilves M., Hartig A., Gurvitz A., Hiltunen J.K.; "Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers."; J. Biol. Chem. 278:41213-41220(2003).
[3]	X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND MUTAGENESIS OF TYR-79. DOI=10.1016/S0022-2836(03)00038-X; PubMed=12614607 [NCBI, ExPASy, EBI, Israel, Japan] Airenne T.T., Torkko J.M., Van den plas S., Sormunen R.T., Kastaniotis A.J., Wierenga R.K., Hiltunen J.K.; "Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance."; J. Mol. Biol. 327:47-59(2003).

Comments

FUNCTION: Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.
CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NADP⁺ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH.
CATALYTIC ACTIVITY: Acyl-CoA + NADP⁺ = trans-2,3-dehydroacyl-CoA + NADPH.
SUBUNIT: Homodimer and heterodimer with etr2.
SUBCELLULAR LOCATION: Mitochondrion.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

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

U94997; AAL55472.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1GU7; X-ray; 1.70 A; A/B=23-386.	[ExPASy / RCSB / EBI]
1GUF; X-ray; 2.25 A; A/B=23-386.	[ExPASy / RCSB / EBI]
1GYR; X-ray; 2.60 A; A/B/C=23-386.	[ExPASy / RCSB / EBI]
1N9G; X-ray; 1.98 A; B/D/E=1-386.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1GU7; -.
1GUF; -.
1GYR; -.
1N9G; -.

ModBase

Q8WZM3.

Protein-protein interaction databases

IntAct

Q8WZM3; -.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
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.
Pfam graphical view of domain structure.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; Oxidoreductase; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 22`	`22`	`Mitochondrion.`
`CHAIN`	`23 386`	`364`	`Enoyl-[acyl-carrier-protein] reductase [NADPH, B-specific] 1, mitochondrial.`	`PRO_0000000898`
`MUTAGEN`	`79 79`		`Y->N: 0.1% of catalytic activity.`
`STRAND`	`24 33`	`10`
`HELIX`	`37 40`	`4`
`STRAND`	`42 48`	`7`
`STRAND`	`57 67`	`11`
`HELIX`	`69 76`	`8`
`STRAND`	`95 97`	`3`
`STRAND`	`103 109`	`7`
`STRAND`	`121 127`	`7`
`STRAND`	`132 139`	`8`
`HELIX`	`140 142`	`3`
`STRAND`	`143 146`	`4`
`HELIX`	`149 154`	`6`
`HELIX`	`163 167`	`5`
`HELIX`	`172 181`	`10`
`STRAND`	`182 184`	`3`
`TURN`	`188 190`	`3`
`STRAND`	`192 196`	`5`
`HELIX`	`201 213`	`13`
`STRAND`	`216 221`	`6`
`HELIX`	`227 237`	`11`
`STRAND`	`240 244`	`5`
`HELIX`	`245 249`	`5`
`HELIX`	`251 253`	`3`
`HELIX`	`254 264`	`11`
`STRAND`	`268 275`	`8`
`HELIX`	`277 285`	`9`
`STRAND`	`292 295`	`4`
`STRAND`	`304 306`	`3`
`HELIX`	`308 313`	`6`
`STRAND`	`317 320`	`4`
`HELIX`	`323 327`	`5`
`HELIX`	`331 346`	`16`
`STRAND`	`356 359`	`4`
`STRAND`	`362 364`	`3`
`HELIX`	`366 375`	`10`
`HELIX`	`377 379`	`3`
`STRAND`	`382 385`	`4`

Sequence information

Length: 386 AA [This is the length of the unprocessed precursor]

Molecular weight: 42161 Da [This is the MW of the unprocessed precursor]

CRC64: FCBC174A240742D8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYSVLKQSIR PRLLATHNQF RTMITAQAVL YTQHGEPKDV LFTQSFEIDD DNLAPNEVIV 

        70         80         90        100        110        120 
KTLGSPVNPS DINQIQGVYP SKPAKTTGFG TTEPAAPCGN 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 REFGPTIKEW IKQSGGEAKL ALNCVGGKSS TGIARKLNNN GLMLTYGGMS 

       310        320        330        340        350        360 
FQPVTIPTSL YIFKNFTSAG FWVTELLKNN KELKTSTLNQ IIAWYEEGKL TDAKSIETLY 

       370        380 
DGTKPLHELY QDGVANSKDG KQLITY

Q8WZM3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools