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Database: UniProt
Entry: K9QXG7_NOSS7
LinkDB: K9QXG7_NOSS7
Original site: K9QXG7_NOSS7 
ID   K9QXG7_NOSS7            Unreviewed;       148 AA.
AC   K9QXG7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA hydrolase {ECO:0000256|HAMAP-Rule:MF_02101};
DE            Short=DHNA-CoA hydrolase {ECO:0000256|HAMAP-Rule:MF_02101};
DE            EC=3.1.2.28 {ECO:0000256|HAMAP-Rule:MF_02101};
DE   AltName: Full=DHNA-CoA thioesterase {ECO:0000256|HAMAP-Rule:MF_02101};
GN   OrderedLocusNames=Nos7524_4562 {ECO:0000313|EMBL:AFY50310.1};
OS   Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY50310.1, ECO:0000313|Proteomes:UP000010378};
RN   [1] {ECO:0000313|Proteomes:UP000010378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:0000256|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:0000256|HAMAP-
CC         Rule:MF_02101};
CC   -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_02101}.
CC   -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC       DHNA-CoA hydrolase subfamily. {ECO:0000256|HAMAP-Rule:MF_02101}.
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DR   EMBL; CP003552; AFY50310.1; -; Genomic_DNA.
DR   RefSeq; WP_015140720.1; NC_019684.1.
DR   AlphaFoldDB; K9QXG7; -.
DR   STRING; 28072.Nos7524_4562; -.
DR   KEGG; nop:Nos7524_4562; -.
DR   PATRIC; fig|28072.8.peg.4997; -.
DR   eggNOG; COG0824; Bacteria.
DR   HOGENOM; CLU_101141_5_3_3; -.
DR   OrthoDB; 9800856at2; -.
DR   UniPathway; UPA00995; -.
DR   UniPathway; UPA01057; UER01033.
DR   Proteomes; UP000010378; Chromosome.
DR   GO; GO:0016790; F:thiolester hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00586; 4HBT; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   HAMAP; MF_02101; DHNA_CoA_hydrolase; 1.
DR   InterPro; IPR022829; DHNA_CoA_hydrolase.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR006684; YbgC/YbaW.
DR   PANTHER; PTHR31793; 4-HYDROXYBENZOYL-COA THIOESTERASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR31793:SF27; ACYL-ACYL CARRIER PROTEIN THIOESTERASE ATL1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF13279; 4HBT_2; 1.
DR   PIRSF; PIRSF003230; YbgC; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02101};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010378}.
FT   ACT_SITE        15
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02101"
SQ   SEQUENCE   148 AA;  16859 MW;  C3E254F2B7DA6290 CRC64;
     MSFTYHRTVR FQDTDAAGVV YFAHVLSICH EAYEESLGMS GINIKEFFTQ PKVAFPIVHA
     SVDFLRPIFC GDKLLISLMP QKIGAEKFEI TYEISSDEVI FAKAITRHVC IDASSRSKQE
     LPTDIIQWLE SNRKETEGAE RRKAREAI
//
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