DNAT2_ARATH
ID DNAT2_ARATH Reviewed; 157 AA.
AC Q9FI76;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA thioesterase 2 {ECO:0000303|PubMed:22372525};
DE Short=AtDHNAT2 {ECO:0000303|PubMed:22372525};
DE Short=DHNA-CoA thioesterase 2 {ECO:0000303|PubMed:22372525};
DE EC=3.1.2.- {ECO:0000305};
GN Name=DHNAT2 {ECO:0000303|PubMed:22372525};
GN OrderedLocusNames=At5g48950 {ECO:0000312|Araport:AT5G48950};
GN ORFNames=K19E20.6 {ECO:0000312|EMBL:BAB10318.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista-Mercan V.R., Kim C.J., Chen H., Quan R., De Los Reyes C.,
RA Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP WEB RESOURCE.
RX PubMed=15333753; DOI=10.1104/pp.104.043695;
RA Reumann S., Ma C., Lemke S., Babujee L.;
RT "AraPerox. A database of putative Arabidopsis proteins from plant
RT peroxisomes.";
RL Plant Physiol. 136:2587-2608(2004).
RN [5]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP MISCELLANEOUS.
RX PubMed=22372525; DOI=10.1111/j.1365-313x.2012.04972.x;
RA Widhalm J.R., Ducluzeau A.-L., Buller N.E., Elowsky C.G., Olsen L.J.,
RA Basset G.J.C.;
RT "Phylloquinone (vitamin K(1)) biosynthesis in plants: two peroxisomal
RT thioesterases of Lactobacillales origin hydrolyze 1,4-dihydroxy-2-
RT naphthoyl-CoA.";
RL Plant J. 71:205-215(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of the thioester bond of 1,4-
CC dihydroxy-2-naphthoyl-CoA (DHNA-CoA) in peroxisomes, a necessary step
CC to form the naphthoquinone ring of phylloquinone (vitamin K(1)).
CC Displayed also slight thioesterase activity towards benzoyl-CoA. Is not
CC active on phenylacetyl-CoA, succinyl-CoA and palmitoyl-CoA thioesters.
CC {ECO:0000269|PubMed:22372525}.
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000305|PubMed:22372525}.
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 7/7.
CC {ECO:0000305|PubMed:22372525}.
CC -!- SUBUNIT: Homotetramers. {ECO:0000250|UniProtKB:Q9SX65}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:22372525}.
CC -!- DISRUPTION PHENOTYPE: Reduced DHNA-CoA thioesterase activity and
CC phylloquinone content. {ECO:0000269|PubMed:22372525}.
CC -!- MISCELLANEOUS: May originate from a horizontal gene transfer with a
CC bacterial species of the Lactobacillales order.
CC {ECO:0000303|PubMed:22372525}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC DHNA-CoA hydrolase subfamily. {ECO:0000305}.
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DR EMBL; AB017061; BAB10318.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95748.1; -; Genomic_DNA.
DR EMBL; BT030605; ABR46185.1; -; mRNA.
DR RefSeq; NP_199706.1; NM_124272.3.
DR AlphaFoldDB; Q9FI76; -.
DR SMR; Q9FI76; -.
DR STRING; 3702.AT5G48950.1; -.
DR PaxDb; Q9FI76; -.
DR PRIDE; Q9FI76; -.
DR ProteomicsDB; 220713; -.
DR EnsemblPlants; AT5G48950.1; AT5G48950.1; AT5G48950.
DR GeneID; 834953; -.
DR Gramene; AT5G48950.1; AT5G48950.1; AT5G48950.
DR KEGG; ath:AT5G48950; -.
DR Araport; AT5G48950; -.
DR TAIR; locus:2154354; AT5G48950.
DR eggNOG; KOG3328; Eukaryota.
DR HOGENOM; CLU_089876_2_0_1; -.
DR InParanoid; Q9FI76; -.
DR OMA; SIHHIRP; -.
DR OrthoDB; 1518904at2759; -.
DR PhylomeDB; Q9FI76; -.
DR BioCyc; ARA:AT5G48950-MON; -.
DR BioCyc; MetaCyc:AT5G48950-MON; -.
DR BRENDA; 3.1.2.28; 399.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER01033.
DR PRO; PR:Q9FI76; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI76; baseline and differential.
DR Genevisible; Q9FI76; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0061522; F:1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity; IBA:GO_Central.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IMP:TAIR.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR00369; unchar_dom_1; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Peroxisome; Reference proteome.
FT CHAIN 1..157
FT /note="1,4-dihydroxy-2-naphthoyl-CoA thioesterase 2"
FT /id="PRO_0000432100"
FT MOTIF 154..156
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 56
FT /evidence="ECO:0000250|UniProtKB:Q9SX65"
SQ SEQUENCE 157 AA; 17063 MW; F078ABECE9B3C35F CRC64;
MDPKSPEFII DQPLKILGFV FDELSATRVS GHLTLTEKCC QPFKVLHGGV SALIAEALAS
LGAGIASGFK RVAGIHLSIH HLRPAALGEI VFAESFPVSV GKNIQVWEVR LWKAKKTETP
DNKIMVSTSR VTLFCGLPIP DHVKDAPDEL KKVISKL
