FATB_UMBCA
ID FATB_UMBCA Reviewed; 382 AA.
AC Q41635;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Dodecanoyl-[acyl-carrier-protein] hydrolase, chloroplastic {ECO:0000305};
DE EC=3.1.2.21 {ECO:0000269|PubMed:1621095, ECO:0000269|PubMed:28991437};
DE AltName: Full=12:0-acyl-carrier protein thioesterase;
DE Short=12:0-ACP thioesterase;
DE AltName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE AltName: Full=BTE;
DE AltName: Full=Lauroyl-acyl carrier protein thioesterase;
DE AltName: Full=UcFatB1 {ECO:0000303|PubMed:7479856};
DE Flags: Precursor;
GN Name=FATB1 {ECO:0000303|PubMed:7479856}; Synonyms=FATB;
OS Umbellularia californica (California bay laurel) (Tetranthera californica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae;
OC Umbellularia.
OX NCBI_TaxID=3438;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 84-91, FUNCTION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=1621095; DOI=10.1126/science.1621095;
RA Voelker T.A., Worrell A.C., Anderson L., Bleibaum J., Fan C., Hawkins D.J.,
RA Radke S.E., Davies H.M.;
RT "Fatty acid biosynthesis redirected to medium chains in transgenic oilseed
RT plants.";
RL Science 257:72-74(1992).
RN [2]
RP FUNCTION, MUTAGENESIS OF MET-197; ARG-199; THR-231 AND ARG-327, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7479856; DOI=10.1073/pnas.92.23.10639;
RA Yuan L., Voelker T.A., Hawkins D.J.;
RT "Modification of the substrate specificity of an acyl-acyl carrier protein
RT thioesterase by protein engineering.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10639-10643(1995).
RN [3]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 97-365, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVE SITE, SUBUNIT, AND MUTAGENESIS OF GLU-135; THR-137;
RP MET-163; MET-197; ARG-199; PHE-201; SER-219; ARG-276; ASP-281; ASN-283;
RP HIS-285; GLU-319 AND CYS-320.
RX PubMed=28991437; DOI=10.1021/acschembio.7b00641;
RA Feng Y., Wang Y., Liu J., Liu Y., Cao X., Xue S.;
RT "Structural insight into acyl-ACP thioesterase toward substrate specificity
RT design.";
RL ACS Chem. Biol. 12:2830-2836(2017).
CC -!- FUNCTION: Plays an essential role in chain termination during de novo
CC fatty acid synthesis. High thioesterase activity for lauroyl-ACP versus
CC other acyl-ACPs. {ECO:0000269|PubMed:1621095,
CC ECO:0000269|PubMed:28991437, ECO:0000269|PubMed:7479856}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-[ACP] + H2O = dodecanoate + H(+) + holo-[ACP];
CC Xref=Rhea:RHEA:30119, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:65264; EC=3.1.2.21;
CC Evidence={ECO:0000269|PubMed:1621095, ECO:0000269|PubMed:28991437};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for 12:0-[acyl-carrier-protein]
CC {ECO:0000269|PubMed:7479856};
CC KM=6.4 uM for 14:0-[acyl-carrier-protein]
CC {ECO:0000269|PubMed:7479856};
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:28991437}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000303|PubMed:1621095}.
CC -!- TISSUE SPECIFICITY: Expressed in developing cotyledons. Not detected in
CC leaves. {ECO:0000303|PubMed:1621095}.
CC -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
CC canola by Monsanto (Calgene) so as to obtain laurate-rich seeds.
CC -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
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DR EMBL; M94159; AAA34215.1; -; mRNA.
DR PIR; A40229; A40229.
DR PDB; 5X04; X-ray; 2.43 A; A/B=97-365.
DR PDBsum; 5X04; -.
DR AlphaFoldDB; Q41635; -.
DR SMR; Q41635; -.
DR BRENDA; 3.1.2.14; 6562.
DR BRENDA; 3.1.2.21; 6562.
DR SABIO-RK; Q41635; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0047381; F:dodecanoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR021113; Acyl-ACP-thioesterase_N.
DR InterPro; IPR002864; Acyl-ACP_thioesterase.
DR InterPro; IPR045023; FATA/B.
DR InterPro; IPR029069; HotDog_dom_sf.
DR PANTHER; PTHR31727; PTHR31727; 1.
DR Pfam; PF01643; Acyl-ACP_TE; 1.
DR Pfam; PF12590; Acyl-thio_N; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Genetically modified food;
KW Hydrolase; Lipid biosynthesis; Lipid metabolism; Plastid; Transit peptide.
FT TRANSIT 1..83
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1621095"
FT CHAIN 84..382
FT /note="Dodecanoyl-[acyl-carrier-protein] hydrolase,
FT chloroplastic"
FT /id="PRO_0000000591"
FT ACT_SITE 283
FT /evidence="ECO:0000269|PubMed:28991437"
FT ACT_SITE 285
FT /evidence="ECO:0000269|PubMed:28991437"
FT ACT_SITE 320
FT /evidence="ECO:0000255"
FT SITE 281
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:28991437"
FT SITE 283
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:28991437"
FT SITE 285
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:28991437"
FT SITE 319
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 135
FT /note="E->Q: Loss of catalytic activity, when associated
FT with E-276."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 137
FT /note="T->G: Increases C14 substrate selectivity."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 137
FT /note="T->Y: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 163
FT /note="M->W: Reduces catalytic activity 75-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 197
FT /note="M->R: Converted to a 12:0/14:0 ACP TE with equal
FT preference for both substrates; when associated with H-199.
FT Converted to a 14:0 ACP TE; when associated with H-199 and
FT K-231."
FT /evidence="ECO:0000269|PubMed:7479856"
FT MUTAGEN 197
FT /note="M->R: Reduces catalytic activity 2.5-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 199
FT /note="R->H: Converted to a 12:0/14:0 ACP TE with equal
FT preference for both substrates; when associated with R-197.
FT Converted to a 14:0 ACP TE; when associated with R-197 and
FT K-231."
FT /evidence="ECO:0000269|PubMed:7479856"
FT MUTAGEN 199
FT /note="R->H: Reduces catalytic activity 250-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 201
FT /note="F->W: Reduces catalytic activity 7-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 219
FT /note="S->W: Reduces catalytic activity 75-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 231
FT /note="T->K: No effect on specificity. Converted to a 14:0
FT ACP TE; when associated with R-197 and H-199."
FT /evidence="ECO:0000269|PubMed:7479856"
FT MUTAGEN 276
FT /note="R->E: Loss of catalytic activity, when associated
FT with Q-135."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 281
FT /note="D->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 283
FT /note="N->A: Reduces catalytic activity 33-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 285
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 319
FT /note="E->A: Reduces catalytic activity 33-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 320
FT /note="C->A: Reduces catalytic activity 3-fold."
FT /evidence="ECO:0000269|PubMed:28991437"
FT MUTAGEN 327
FT /note="R->Q: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:7479856"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 162..174
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:5X04"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 196..205
FT /evidence="ECO:0007829|PDB:5X04"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 211..223
FT /evidence="ECO:0007829|PDB:5X04"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:5X04"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 307..316
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:5X04"
FT STRAND 354..364
FT /evidence="ECO:0007829|PDB:5X04"
SQ SEQUENCE 382 AA; 42915 MW; 96262A558545E89F CRC64;
MATTSLASAF CSMKAVMLAR DGRGMKPRSS DLQLRAGNAP TSLKMINGTK FSYTESLKRL
PDWSMLFAVI TTIFSAAEKQ WTNLEWKPKP KLPQLLDDHF GLHGLVFRRT FAIRSYEVGP
DRSTSILAVM NHMQEATLNH AKSVGILGDG FGTTLEMSKR DLMWVVRRTH VAVERYPTWG
DTVEVECWIG ASGNNGMRRD FLVRDCKTGE ILTRCTSLSV LMNTRTRRLS TIPDEVRGEI
GPAFIDNVAV KDDEIKKLQK LNDSTADYIQ GGLTPRWNDL DVNQHVNNLK YVAWVFETVP
DSIFESHHIS SFTLEYRREC TRDSVLRSLT TVSGGSSEAG LVCDHLLQLE GGSEVLRART
EWRPKLTDSF RGISVIPAEP RV
