DNCH_THEVB
ID DNCH_THEVB Reviewed; 146 AA.
AC Q8DLK3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA hydrolase {ECO:0000255|HAMAP-Rule:MF_02101};
DE Short=DHNA-CoA hydrolase {ECO:0000255|HAMAP-Rule:MF_02101};
DE EC=3.1.2.28 {ECO:0000255|HAMAP-Rule:MF_02101};
DE AltName: Full=DHNA-CoA thioesterase {ECO:0000255|HAMAP-Rule:MF_02101};
GN OrderedLocusNames=tll0488;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA
CC (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a reaction involved in
CC phylloquinone (vitamin K1) biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_02101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-
CC naphthoate + CoA + H(+); Xref=Rhea:RHEA:26309, ChEBI:CHEBI:11173,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58897; EC=3.1.2.28; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02101};
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02101}.
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 7/7.
CC {ECO:0000255|HAMAP-Rule:MF_02101}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC DHNA-CoA hydrolase subfamily. {ECO:0000255|HAMAP-Rule:MF_02101}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000039; BAC08040.1; -; Genomic_DNA.
DR RefSeq; NP_681278.1; NC_004113.1.
DR AlphaFoldDB; Q8DLK3; -.
DR SMR; Q8DLK3; -.
DR STRING; 197221.22294209; -.
DR EnsemblBacteria; BAC08040; BAC08040; BAC08040.
DR KEGG; tel:tll0488; -.
DR PATRIC; fig|197221.4.peg.513; -.
DR eggNOG; COG0824; Bacteria.
DR OMA; IVNCEAN; -.
DR OrthoDB; 1786865at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER01033.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02101; DHNA_CoA_hydrolase; 1.
DR InterPro; IPR022829; DHNA_CoA_hydrolase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006684; YbgC/YbaW.
DR PIRSF; PIRSF003230; YbgC; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..146
FT /note="1,4-dihydroxy-2-naphthoyl-CoA hydrolase"
FT /id="PRO_0000377036"
FT ACT_SITE 19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02101"
SQ SEQUENCE 146 AA; 16719 MW; C12FD8032D222F5B CRC64;
MNPTPLRDYQ RTVHFADTDA AGVVYFANLL RFCHEAYEDA LAQLGVDLRQ FFSNSGLIVP
ITEAQIRFLK PLYCGDRLRV TIDPQRLDTS RFQLTYTLYN EGGDRVAIAQ TQHMCLQLPH
RQRVPIPDPL PAWLKSAPEE ASDRED
