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Database: UniProt
Entry: W0EAL6_9FIRM
LinkDB: W0EAL6_9FIRM
Original site: W0EAL6_9FIRM 
ID   W0EAL6_9FIRM            Unreviewed;       279 AA.
AC   W0EAL6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase {ECO:0000256|HAMAP-Rule:MF_01934};
DE            Short=DHNA-CoA synthase {ECO:0000256|HAMAP-Rule:MF_01934};
DE            EC=4.1.3.36 {ECO:0000256|HAMAP-Rule:MF_01934};
GN   Name=menB {ECO:0000256|HAMAP-Rule:MF_01934};
GN   ORFNames=DESME_13415 {ECO:0000313|EMBL:AHF07910.1};
OS   Desulfitobacterium metallireducens DSM 15288.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF07910.1, ECO:0000313|Proteomes:UP000010847};
RN   [1] {ECO:0000313|EMBL:AHF07910.1, ECO:0000313|Proteomes:UP000010847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG   DOE Joint Genome Institute;
RA   Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-
CC       naphthoyl-CoA (DHNA-CoA). {ECO:0000256|HAMAP-Rule:MF_01934}.
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         Evidence={ECO:0000256|ARBA:ARBA00000177, ECO:0000256|HAMAP-
CC         Rule:MF_01934};
CC   -!- COFACTOR:
CC       Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01934};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7.
CC       {ECO:0000256|HAMAP-Rule:MF_01934}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01934}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01934}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01934}.
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DR   EMBL; CP007032; AHF07910.1; -; Genomic_DNA.
DR   RefSeq; WP_006715837.1; NZ_CP007032.1.
DR   AlphaFoldDB; W0EAL6; -.
DR   STRING; 871968.DESME_13415; -.
DR   KEGG; dmt:DESME_13415; -.
DR   eggNOG; COG0447; Bacteria.
DR   HOGENOM; CLU_009834_7_7_9; -.
DR   OrthoDB; 9775794at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00167.
DR   Proteomes; UP000010847; Chromosome.
DR   GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 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   NCBIfam; TIGR01929; menB; 1.
DR   PANTHER; PTHR43113:SF1; 1,4-DIHYDROXY-2-NAPHTHOYL-COA SYNTHASE, PEROXISOMAL; 1.
DR   PANTHER; PTHR43113; NUCLEOSIDE-DIPHOSPHATE-SUGAR EPIMERASE; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01934, ECO:0000313|EMBL:AHF07910.1};
KW   Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW   Rule:MF_01934}; Reference proteome {ECO:0000313|Proteomes:UP000010847}.
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         79..83
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         123..127
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         148..150
FT                   /ligand="hydrogencarbonate"
FT                   /ligand_id="ChEBI:CHEBI:17544"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   SITE            91
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT   SITE            252
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
SQ   SEQUENCE   279 AA;  31286 MW;  DAF7DC39A35DE71C CRC64;
     MNFPWKQLNR NYEDIRYEIY DGIAKITINR PEVRNAFRPK TIMELMDAFT VAREDRQIGV
     IILTGANHGQ GQDKEAFCSG GDQRVRGNGG YVGDDQIPRL NVLDLQHLIR IIPKPVIAMV
     NGFAIGGGHV LHIVCDLSIA SENAKFGQTG PKVGSFDAGY GAGYLARIVG HKKAREIWYL
     CRQYTAQEAL EMGLVNTVVP FEQLEEETVK WAKEILQHSP TALRFLKASF NADTDGLAGL
     QQFAGDATLL YYTSEEAKEG RDAYLEKRKP DFEQFPKFP
//
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