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