DNCH_PROMA
ID DNCH_PROMA Reviewed; 155 AA.
AC Q7VE16;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Pro_0198;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAP99244.1; -; Genomic_DNA.
DR RefSeq; NP_874592.1; NC_005042.1.
DR RefSeq; WP_011124353.1; NC_005042.1.
DR AlphaFoldDB; Q7VE16; -.
DR SMR; Q7VE16; -.
DR STRING; 167539.Pro_0198; -.
DR EnsemblBacteria; AAP99244; AAP99244; Pro_0198.
DR GeneID; 54199557; -.
DR KEGG; pma:Pro_0198; -.
DR PATRIC; fig|167539.5.peg.205; -.
DR eggNOG; COG0824; Bacteria.
DR HOGENOM; CLU_101141_5_3_3; -.
DR OMA; IVNCEAN; -.
DR OrthoDB; 1786865at2; -.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER01033.
DR Proteomes; UP000001420; 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..155
FT /note="1,4-dihydroxy-2-naphthoyl-CoA hydrolase"
FT /id="PRO_0000377015"
FT ACT_SITE 22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02101"
SQ SEQUENCE 155 AA; 17559 MW; BFC5B82E928160E0 CRC64;
MQSKTLQNWL HLQRIVRFGD TDAAGVIHFH QLLRWSHEAW EESLDRYGLK AVDVFPSSLG
ISTSTSVALP IVHCEADFFL PIGIGDKLNV QLVPVRLNIG SFEVQFTFQR REQNVAVALV
RHRSIDSDSR RLCDLPEGID RWLEASSLHR GVSAI
