DNAT1_ARATH
ID DNAT1_ARATH Reviewed; 156 AA.
AC Q9SX65;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1 {ECO:0000303|PubMed:22372525};
DE Short=AtDHNAT1 {ECO:0000303|PubMed:22372525};
DE Short=DHNA-CoA thioesterase 1 {ECO:0000303|PubMed:22372525};
DE EC=3.1.2.- {ECO:0000305};
GN Name=DHNAT1 {ECO:0000303|PubMed:22372525};
GN OrderedLocusNames=At1g48320 {ECO:0000312|Araport:AT1G48320};
GN ORFNames=F11A17.13 {ECO:0000312|EMBL:AAD49765.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=14701923; DOI=10.1093/pcp/pcg173;
RA Kamada T., Nito K., Hayashi H., Mano S., Hayashi M., Nishimura M.;
RT "Functional differentiation of peroxisomes revealed by expression profiles
RT of peroxisomal genes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:1275-1289(2003).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19329564; DOI=10.1104/pp.109.137703;
RA Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT in vivo subcellular targeting verification indicates novel metabolic and
RT regulatory functions of peroxisomes.";
RL Plant Physiol. 150:125-143(2009).
RN [8]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=24100308; DOI=10.1107/s0907444913015771;
RA Furt F., Allen W.J., Widhalm J.R., Madzelan P., Rizzo R.C., Basset G.,
RA Wilson M.A.;
RT "Functional convergence of structurally distinct thioesterases from
RT cyanobacteria and plants involved in phylloquinone biosynthesis.";
RL Acta Crystallogr. D 69:1876-1888(2013).
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)). Is not
CC active on benzoyl-CoA, phenylacetyl-CoA, succinyl-CoA and palmitoyl-CoA
CC thioesters. {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:0000269|PubMed:24100308}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19329564,
CC ECO:0000269|PubMed:22372525}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, stems, leaves and
CC siliques. {ECO:0000269|PubMed:14701923}.
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; AC007932; AAD49765.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32274.1; -; Genomic_DNA.
DR EMBL; BT010185; AAQ22654.1; -; mRNA.
DR EMBL; AK229541; BAF01394.1; -; mRNA.
DR PIR; B96523; B96523.
DR RefSeq; NP_175266.1; NM_103729.3.
DR PDB; 4K02; X-ray; 1.90 A; A/B=1-156.
DR PDBsum; 4K02; -.
DR AlphaFoldDB; Q9SX65; -.
DR SMR; Q9SX65; -.
DR IntAct; Q9SX65; 1.
DR STRING; 3702.AT1G48320.1; -.
DR PaxDb; Q9SX65; -.
DR PRIDE; Q9SX65; -.
DR ProteomicsDB; 222157; -.
DR EnsemblPlants; AT1G48320.1; AT1G48320.1; AT1G48320.
DR GeneID; 841252; -.
DR Gramene; AT1G48320.1; AT1G48320.1; AT1G48320.
DR KEGG; ath:AT1G48320; -.
DR Araport; AT1G48320; -.
DR TAIR; locus:2007735; AT1G48320.
DR eggNOG; KOG3328; Eukaryota.
DR HOGENOM; CLU_089876_2_0_1; -.
DR InParanoid; Q9SX65; -.
DR OMA; CNLPIPD; -.
DR OrthoDB; 1518904at2759; -.
DR PhylomeDB; Q9SX65; -.
DR BRENDA; 3.1.2.28; 399.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER01033.
DR PRO; PR:Q9SX65; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SX65; differential.
DR Genevisible; Q9SX65; 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; IDA: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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Peroxisome; Reference proteome.
FT CHAIN 1..156
FT /note="1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1"
FT /id="PRO_0000432099"
FT MOTIF 154..156
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 57
FT /evidence="ECO:0000305|PubMed:24100308"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:4K02"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:4K02"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4K02"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4K02"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4K02"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:4K02"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:4K02"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:4K02"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:4K02"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:4K02"
SQ SEQUENCE 156 AA; 16713 MW; 986C79FC0F985B23 CRC64;
MDSASSNTKA IDPPLHMLGF EFDELSPTRI TGRLPVSPVC CQPFKVLHGG VSALIAESLA
SMGAHMASGF KRVAGIQLSI NHLKSADLGD LVFAEATPVS TGKTIQVWEV KLWKTTQKDK
ANKILISSSR VTLICNLPIP DNAKDAANML KMVAKL
