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Database: UniProt
Entry: V4L8F9_EUTSA
LinkDB: V4L8F9_EUTSA
Original site: V4L8F9_EUTSA 
ID   V4L8F9_EUTSA            Unreviewed;       412 AA.
AC   V4L8F9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Acyl-[acyl-carrier-protein] hydrolase {ECO:0000256|RuleBase:RU363096};
DE            EC=3.1.2.- {ECO:0000256|RuleBase:RU363096};
GN   ORFNames=EUTSA_v10007761mg {ECO:0000313|EMBL:ESQ36033.1};
OS   Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX   NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ36033.1, ECO:0000313|Proteomes:UP000030689};
RN   [1] {ECO:0000313|EMBL:ESQ36033.1, ECO:0000313|Proteomes:UP000030689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA   Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA   Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA   Mitchell-Olds T., Schumaker K.S., Wang X.;
RT   "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL   Front. Plant Sci. 4:46-46(2013).
CC   -!- FUNCTION: Plays an essential role in chain termination during de novo
CC       fatty acid synthesis. {ECO:0000256|RuleBase:RU363096}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|RuleBase:RU363096}.
CC   -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family.
CC       {ECO:0000256|ARBA:ARBA00006500, ECO:0000256|RuleBase:RU363096}.
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DR   EMBL; KI517683; ESQ36033.1; -; Genomic_DNA.
DR   RefSeq; XP_006417680.1; XM_006417617.1.
DR   AlphaFoldDB; V4L8F9; -.
DR   STRING; 72664.V4L8F9; -.
DR   EnsemblPlants; ESQ36033; ESQ36033; EUTSA_v10007761mg.
DR   GeneID; 18994024; -.
DR   Gramene; ESQ36033; ESQ36033; EUTSA_v10007761mg.
DR   KEGG; eus:EUTSA_v10007761mg; -.
DR   eggNOG; ENOG502QQHW; Eukaryota.
DR   OMA; NSGRMKV; -.
DR   OrthoDB; 1207631at2759; -.
DR   Proteomes; UP000030689; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:EnsemblPlants.
DR   GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:EnsemblPlants.
DR   CDD; cd00586; 4HBT; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   InterPro; IPR021113; Acyl-ACP-thioesterase_N.
DR   InterPro; IPR049427; Acyl-ACP_TE_C.
DR   InterPro; IPR002864; Acyl-ACP_thioesterase_NHD.
DR   InterPro; IPR045023; FATA/B.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   PANTHER; PTHR31727; OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31727:SF2; PALMITOYL-ACYL CARRIER PROTEIN THIOESTERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01643; Acyl-ACP_TE; 1.
DR   Pfam; PF20791; Acyl-ACP_TE_C; 1.
DR   Pfam; PF12590; Acyl-thio_N; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|RuleBase:RU363096};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU363096};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU363096};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363096};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU363096};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU363096};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|RuleBase:RU363096};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030689};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          1..124
FT                   /note="Acyl-ACP-thioesterase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12590"
FT   DOMAIN          135..270
FT                   /note="Acyl-ACP thioesterase N-terminal hotdog"
FT                   /evidence="ECO:0000259|Pfam:PF01643"
FT   DOMAIN          296..399
FT                   /note="Acyl-ACP thioesterase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20791"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  45797 MW;  A5CE30948BCB5EAB CRC64;
     MVATSATSSF FPVPSPSLDP NGKGSKVAST NFAGLNSTPN SGRMKVKPNA QAPPKINGKK
     VGLPGSVELL KTDNETSHPA PRTFINQLPD WSMLLAAITT VFLAAEKQWM MLDWKPRRSD
     MIMDPFGLGR IVQDGLVFRQ NFSIRSYEIG ADRSASIETV MNHLQETALN HVKSAGLLGD
     GFGSTPEMFK KNLIWVVTRM QVVVDKYPTW GDVVEVDTWV SQSGKNGMRR DWLVRDCNTG
     EILTRASSVW VMMNKLTRRL SKIPEEVRGE IEPYFVNSDP VLAEDSRKLT KLDDKTADYV
     RSGLTPRWSD LDVNQHVNNV KYIGWILESA PVGMMERQKL KSMTLEYRRE CGRDSVLQSL
     TAVSGCDIGN LGTAGEVECQ HLLRLQDGAE VVRGRTEWSS KTPTTTWGTT PS
//
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