DNCH_SYNY3
ID DNCH_SYNY3 Reviewed; 138 AA.
AC Q55777;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=slr0204;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP FUNCTION IN PHYLLOQUINONE BIOSYNTHESIS, CATALYTIC ACTIVITY, PATHWAY,
RP SUBSTRATE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19321747; DOI=10.1073/pnas.0900738106;
RA Widhalm J.R., van Oostende C., Furt F., Basset G.J.C.;
RT "A dedicated thioesterase of the Hotdog-fold family is required for the
RT biosynthesis of the naphthoquinone ring of vitamin K1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5599-5603(2009).
CC -!- FUNCTION: Catalyzes the specific hydrolysis of 1,4-dihydroxy-2-
CC naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a
CC reaction involved in phylloquinone (vitamin K1) biosynthesis. Is not
CC active on benzoyl-CoA, phenylacetyl-CoA and aliphatic acyl-CoA
CC thioesters. {ECO:0000269|PubMed:19321747}.
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, ECO:0000269|PubMed:19321747};
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02101, ECO:0000269|PubMed:19321747}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate DHNA-CoA, lack
CC phylloquinone, and display photosensitivity to high light intensities.
CC {ECO:0000269|PubMed:19321747}.
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; BA000022; BAA10428.1; -; Genomic_DNA.
DR PIR; S76582; S76582.
DR PDB; 4K00; X-ray; 1.90 A; A/B=1-138.
DR PDBsum; 4K00; -.
DR AlphaFoldDB; Q55777; -.
DR SMR; Q55777; -.
DR IntAct; Q55777; 4.
DR STRING; 1148.1001691; -.
DR PaxDb; Q55777; -.
DR EnsemblBacteria; BAA10428; BAA10428; BAA10428.
DR KEGG; syn:slr0204; -.
DR eggNOG; COG0824; Bacteria.
DR InParanoid; Q55777; -.
DR OMA; IVNCEAN; -.
DR PhylomeDB; Q55777; -.
DR BioCyc; MetaCyc:MON-15406; -.
DR BRENDA; 3.1.2.28; 382.
DR UniPathway; UPA00995; -.
DR UniPathway; UPA01057; UER01033.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IMP:UniProtKB.
DR HAMAP; MF_02101; DHNA_CoA_hydrolase; 1.
DR InterPro; IPR022829; DHNA_CoA_hydrolase.
DR InterPro; IPR008272; HB-CoA_thioesterase_AS.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR InterPro; IPR006684; YbgC/YbaW.
DR Pfam; PF03061; 4HBT; 1.
DR PIRSF; PIRSF003230; YbgC; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..138
FT /note="1,4-dihydroxy-2-naphthoyl-CoA hydrolase"
FT /id="PRO_0000087769"
FT ACT_SITE 16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02101"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4K00"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4K00"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4K00"
FT HELIX 23..40
FT /evidence="ECO:0007829|PDB:4K00"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:4K00"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4K00"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4K00"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:4K00"
FT STRAND 85..97
FT /evidence="ECO:0007829|PDB:4K00"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:4K00"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:4K00"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:4K00"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:4K00"
SQ SEQUENCE 138 AA; 15478 MW; BBF23841B0BE4A41 CRC64;
MGTFTYERQV YLADTDGAGV VYFNQFLQMC HEAYESWLSS EHLSLQNIIS VGDFALPLVH
ASIDFFAPAH CGDRLLVNLT ITQASAHRFC CDYEISQAES AQLLARAQTH HVCIALPERK
KAPLPQPWQT AICDLDHP
