DNCH_PROMM
ID DNCH_PROMM Reviewed; 151 AA.
AC Q7V4A7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=PMT_2055;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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; BX548175; CAE22229.1; -; Genomic_DNA.
DR RefSeq; WP_011131420.1; NC_005071.1.
DR PDB; 2HX5; X-ray; 1.50 A; A=1-151.
DR PDBsum; 2HX5; -.
DR AlphaFoldDB; Q7V4A7; -.
DR SMR; Q7V4A7; -.
DR STRING; 74547.PMT_2055; -.
DR DNASU; 1729478; -.
DR EnsemblBacteria; CAE22229; CAE22229; PMT_2055.
DR KEGG; pmt:PMT_2055; -.
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 EvolutionaryTrace; Q7V4A7; -.
DR Proteomes; UP000001423; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..151
FT /note="1,4-dihydroxy-2-naphthoyl-CoA hydrolase"
FT /id="PRO_0000377022"
FT ACT_SITE 19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02101"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:2HX5"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2HX5"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2HX5"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2HX5"
FT HELIX 28..44
FT /evidence="ECO:0007829|PDB:2HX5"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2HX5"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2HX5"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:2HX5"
FT STRAND 84..95
FT /evidence="ECO:0007829|PDB:2HX5"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:2HX5"
FT STRAND 110..120
FT /evidence="ECO:0007829|PDB:2HX5"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2HX5"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:2HX5"
SQ SEQUENCE 151 AA; 17304 MW; EA9F48E141EBB974 CRC64;
MNPENWLLLR RVVRFGDTDA AGVMHFHQLF RWCHESWEES LESYGLNPAD IFPGSRKSEV
TPEVALPIIH CQADFRRPIH TGDALAMELR PERLNPNSFQ VHFEFRCEEQ IAAHALIRHL
AINAQTRHRC ALPEGIDRWL EASGVGKIGS I