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Database: UniProt
Entry: A7H762_ANADF
LinkDB: A7H762_ANADF
Original site: A7H762_ANADF 
ID   A7H762_ANADF            Unreviewed;       255 AA.
AC   A7H762;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Acyl-ACP thioesterase {ECO:0000313|EMBL:ABS24558.1};
GN   OrderedLocusNames=Anae109_0343 {ECO:0000313|EMBL:ABS24558.1};
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS24558.1, ECO:0000313|Proteomes:UP000006382};
RN   [1] {ECO:0000313|EMBL:ABS24558.1, ECO:0000313|Proteomes:UP000006382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS24558.1,
RC   ECO:0000313|Proteomes:UP000006382};
RX   PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family.
CC       {ECO:0000256|ARBA:ARBA00006500}.
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DR   EMBL; CP000769; ABS24558.1; -; Genomic_DNA.
DR   RefSeq; WP_011984664.1; NC_009675.1.
DR   AlphaFoldDB; A7H762; -.
DR   STRING; 404589.Anae109_0343; -.
DR   KEGG; afw:Anae109_0343; -.
DR   eggNOG; COG3884; Bacteria.
DR   HOGENOM; CLU_045466_2_0_7; -.
DR   OrthoDB; 9801517at2; -.
DR   Proteomes; UP000006382; Chromosome.
DR   GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31727:SF6; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          3..121
FT                   /note="Acyl-ACP thioesterase N-terminal hotdog"
FT                   /evidence="ECO:0000259|Pfam:PF01643"
FT   DOMAIN          154..243
FT                   /note="Acyl-ACP thioesterase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20791"
SQ   SEQUENCE   255 AA;  28547 MW;  B1CA395BE9D0AA2D CRC64;
     MEKHRQTFGV HTYEVDAFGT VAIAALSGYL QEVAGQHAAA LGVGLEVLMP RGLTWVLARQ
     RIENPVPIVL GDRLEIETWP AGIDRLAALR DFVVRRADGT EVARATTQWF VLDLESRRPV
     KPAEVLDPRF QRELLPPILP LAPGKLPELR SWEFQKRFHV RYGDIDVNMH VTNTSYPTWA
     QEVVPREVFR GQRLASVEVH FLAEAHYGSA ILSRLASTGE GAFAHAIVRE EDEKELARLA
     TRWVPRAAPA VPGAR
//
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