ETR2_CANTR
ID ETR2_CANTR Reviewed; 386 AA.
AC Q8WZM4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase 2, mitochondrial {ECO:0000305};
DE EC=1.3.1.104 {ECO:0000305|PubMed:12890667};
DE AltName: Full=2-enoyl thioester reductase 2 {ECO:0000303|PubMed:12890667};
DE Flags: Precursor;
GN Name=ETR2;
OS Candida tropicalis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5482;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, X-RAY CRYSTALLOGRAPHY
RP (1.98 ANGSTROMS) IN COMPLEX WITH NADP, INDUCTION BY OLEIC ACID, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX PubMed=12890667; DOI=10.1074/jbc.m307664200;
RA Torkko J.M., Koivuranta K.T., Kastaniotis A.J., Airenne T.T., Glumoff T.,
RA Ilves M., Hartig A., Gurvitz A., Hiltunen J.K.;
RT "Candida tropicalis expresses two mitochondrial 2-enoyl thioester
RT reductases that are able to form both homodimers and heterodimers.";
RL J. Biol. Chem. 278:41213-41220(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS).
RA Airenne T.T., Torkko J.M., Hiltunen J.K.;
RT "Crystal structure of enoyl thioester reductase 2.";
RL Submitted (JUN-2002) to the PDB data bank.
CC -!- FUNCTION: Required for respiration and the maintenance of the
CC mitochondrial compartment. Oxidoreductase with a preference for short
CC and medium chain substrates, including trans-2-hexenoyl-CoA (C6),
CC trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May
CC play a role in mitochondrial fatty acid synthesis.
CC {ECO:0000269|PubMed:12890667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.104;
CC Evidence={ECO:0000269|PubMed:12890667};
CC -!- SUBUNIT: Homodimer and heterodimer with ETR1.
CC {ECO:0000269|PubMed:12890667}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- INDUCTION: Up-regulated by growth on oleic acid.
CC {ECO:0000269|PubMed:12890667}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; U94996; AAL55471.1; -; Genomic_DNA.
DR PDB; 1H0K; X-ray; 2.11 A; A/B=23-386.
DR PDB; 1N9G; X-ray; 1.98 A; A/C/F=1-386.
DR PDBsum; 1H0K; -.
DR PDBsum; 1N9G; -.
DR AlphaFoldDB; Q8WZM4; -.
DR SMR; Q8WZM4; -.
DR IntAct; Q8WZM4; 1.
DR VEuPathDB; FungiDB:CTMYA2_052270; -.
DR VEuPathDB; FungiDB:CTRG_06166; -.
DR EvolutionaryTrace; Q8WZM4; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019166; F:trans-2-enoyl-CoA reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Mitochondrion; NADP; Oxidoreductase;
KW Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..386
FT /note="Enoyl-[acyl-carrier-protein] reductase 2,
FT mitochondrial"
FT /id="PRO_0000000899"
FT ACT_SITE 79
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8WZM3"
FT BINDING 172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12890667"
FT BINDING 199..202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12890667"
FT BINDING 222..224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12890667"
FT BINDING 296..299
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12890667"
FT BINDING 321..323
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12890667"
FT BINDING 381
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:12890667"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1H0K"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1N9G"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:1N9G"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 268..275
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:1N9G"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 331..346
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:1N9G"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1N9G"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:1N9G"
SQ SEQUENCE 386 AA; 42117 MW; 91ABE00831F0C2E8 CRC64;
MYSVLKQSIR PRLLATHNQF RTMITAQAVL YTQHGEPKDV LFTQSFEIDD DNLAPNEVIV
KTLGSPINPS DINQIQGVYP SKPAKTTGFG TAEPAAPCGN EGLFEVIKVG SNVSSLEAGD
WVIPSHVNFG TWRTHALGND DDFIKLPNPA QSKANGKPNG LTINQGATIS VNPLTAYLML
THYVKLTPGK DWFIQNGGTS AVGKYASQIG KLLNFNSISV IRDRPNLDEV VASLKELGAT
QVITEDQNNS KEFGPTIKEW IKQSGGEAKL ALNCVGGKSS TGIARKLNNN GLMLTYGGMS
FQPVTIPTSL YIFKNFTSAG FWVTELLKNN KELKTSTLNQ IIAWYEEGKL TDAKSIETLY
DGTKPLHELY QDGVANSKDG KQLITY
