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MENB_CYACA
ID   MENB_CYACA              Reviewed;         268 AA.
AC   Q9TM10;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase;
DE            Short=DHNA-CoA synthase;
DE            EC=4.1.3.36;
GN   Name=menB;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
CC   -!- FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-
CC       naphthoyl-CoA (DHNA-CoA).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA +
CC         H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36;
CC   -!- COFACTOR:
CC       Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544; Evidence={ECO:0000250};
CC       Note=The hydrogencarbonate anion plays the same catalytic role (proton
CC       acceptor) as the side-chain carboxylate group of the essential 'Asp-
CC       185' found in actinobacteria, archaea, bacteroidetes, and
CC       deltaproteobacteria. {ECO:0000250};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF022186; AAF12988.1; -; Genomic_DNA.
DR   RefSeq; NP_045107.1; NC_001840.1.
DR   AlphaFoldDB; Q9TM10; -.
DR   SMR; Q9TM10; -.
DR   GeneID; 800186; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00167.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.12.10; -; 1.
DR   HAMAP; MF_01934; MenB; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR010198; DHNA-CoA_synthase_MenB.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   PANTHER; PTHR43113; PTHR43113; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR01929; menB; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Lyase; Menaquinone biosynthesis; Plastid.
FT   CHAIN           1..268
FT                   /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT                   /id="PRO_0000109329"
FT   BINDING         30..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         70..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         114..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139..141
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            148
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255"
FT   SITE            243
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   268 AA;  29750 MW;  2A18ACEDA4A1F15F CRC64;
     MQTIAIKDFI DIKYIKQDQI SEIIISRPQV LNAFRPRTIN EIIAAFYDSR EDSSIGVVIL
     SGHGSRAFCV GGDQKIRSKT GYIDEKGRSS LNVLELQRII RTFPKPVIAK VSGYAVGGGQ
     ILNMMCDLTI ASENAVLGQS GPKVGSFDAG YGSAYMARII GQKKARELWF TCYQYDAFEA
     YKMGLVNWVV KIEDLDSYAI KLATDILNKS PLAIRFLKSS LNADCDGQSG LQELAGYSTM
     LFYMSAEGQE GHRAFLENRE PDFSKFNS
 
 
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