DNCH_ACAM1
ID DNCH_ACAM1 Reviewed; 137 AA.
AC B0CEN8;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=AM1_3146;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW28143.1; -; Genomic_DNA.
DR RefSeq; WP_010468745.1; NC_009925.1.
DR AlphaFoldDB; B0CEN8; -.
DR SMR; B0CEN8; -.
DR STRING; 329726.AM1_3146; -.
DR EnsemblBacteria; ABW28143; ABW28143; AM1_3146.
DR KEGG; amr:AM1_3146; -.
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; UP000000268; 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..137
FT /note="1,4-dihydroxy-2-naphthoyl-CoA hydrolase"
FT /id="PRO_0000377007"
FT ACT_SITE 12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02101"
SQ SEQUENCE 137 AA; 15556 MW; 4203F6A7120A1EE6 CRC64;
MYTRTVRLQD TDAAGVVYFT SALDICHEAF EDSLMGAGID IRTFFSNPDT ATPIIHADID
FLKPSFCGDQ LTLQLSTHQL AEDEFEVRYN ITAVNKGERL IAKATIRHVC INPINRQRQP
LPKELVTWIQ RWSLAMS