ID   DNCH_PROM4              Reviewed;         151 AA.
AC   A9BD34;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=P9211_01911;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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}.
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DR   EMBL; CP000878; ABX08122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9BD34; -.
DR   SMR; A9BD34; -.
DR   STRING; 93059.P9211_01911; -.
DR   EnsemblBacteria; ABX08122; ABX08122; P9211_01911.
DR   KEGG; pmj:P9211_01911; -.
DR   eggNOG; COG0824; Bacteria.
DR   HOGENOM; CLU_101141_5_3_3; -.
DR   OMA; IVNCEAN; -.
DR   UniPathway; UPA00995; -.
DR   UniPathway; UPA01057; UER01033.
DR   Proteomes; UP000000788; 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   SUPFAM; SSF54637; SSF54637; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..151
FT                   /note="1,4-dihydroxy-2-naphthoyl-CoA hydrolase"
FT                   /id="PRO_0000377017"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02101"
SQ   SEQUENCE   151 AA;  17351 MW;  B8552E0E32562EC8 CRC64;
     MLNSLLPADW LYLERIVRFG ETDSAGVIHF YQLLRWCHES WEESLERYGL KAADVFPNIL
     NKEKQPLVAL PIIHCEADFW KPLQTGDHIS IELLPKKISA GSFQVTFKFK RGDNYVAQAL
     IQHQAINSQT RSCCELSTKI NSWLAESLCI D