ID A0A176VWG5_MARPO Unreviewed; 560 AA.
AC A0A176VWG5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Acyl-[acyl-carrier-protein] hydrolase {ECO:0000256|RuleBase:RU363096};
DE EC=3.1.2.- {ECO:0000256|RuleBase:RU363096};
GN ORFNames=AXG93_3217s1130 {ECO:0000313|EMBL:OAE25097.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25097.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE25097.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25097.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE25097.1}.
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DR EMBL; LVLJ01002403; OAE25097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VWG5; -.
DR OrthoDB; 1207631at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00586; 4HBT; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
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:SF5; ACYL-[ACYL-CARRIER-PROTEIN] HYDROLASE; 1.
DR PANTHER; PTHR31727; OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF01643; Acyl-ACP_TE; 1.
DR Pfam; PF20791; Acyl-ACP_TE_C; 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:UP000077202};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 152..286
FT /note="Acyl-ACP thioesterase N-terminal hotdog"
FT /evidence="ECO:0000259|Pfam:PF01643"
FT DOMAIN 316..380
FT /note="Acyl-ACP thioesterase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20791"
FT REGION 377..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61892 MW; C97B84A0F04AFC7A CRC64;
MDAAAAARCC ALPLPNVALS VAGWTARVRT RSFVPEFGSK KFMTGKALHV GRSTTTHPPR
EGCYDHSARA GLVDGLVDEL LKISKAGGSM VLSNSTLAEP IRQISGGMAL LPSHSESVLR
GILAVVSRPG TLEKPVLTDS VTQGRMMENL LLYRQTFVIR SYEVGADKTA SIETLMNLFQ
ETALNHVRLS GIEGDGFGTT KAMVRNGLIW VVNRMHVEVE SYPAWGDIVE VDSWVASSGK
NGMRRDWMLR DVKTGQILAR ATSTWVMMHQ QTRRLSKMPD DVRAEISSFF LDRHAVPNEG
SMKINKLQND SALYVSSGLQ ARRSDLDMNQ HVNNVKYIAW MMESVPAAYL ENLEIKSITL
EYRRECGQAD VVQSLTNPED MSPASAGSTQ IVNGTRPAES VDPNFPYLSR SPNGVSMLRA
DTPRTLIQES DRLPRFTHLL KLQEGSAEIL DTILSVNREC DAAPKLHCPT VFPESLWIAE
TTCLHNLELA QWCHGLEQRG LRGLRGQLLL SVLVQHSYST LAVASLRRWW NTAMTVAREP
ARVPIPAESS ENRRNGTSEA
//
