ID A0A1I5JLS6_9ACTN Unreviewed; 265 AA.
AC A0A1I5JLS6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05660464_0848 {ECO:0000313|EMBL:SFO73649.1};
OS Geodermatophilus dictyosporus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1523247 {ECO:0000313|EMBL:SFO73649.1, ECO:0000313|Proteomes:UP000198857};
RN [1] {ECO:0000313|Proteomes:UP000198857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44208 {ECO:0000313|Proteomes:UP000198857};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 -!- 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; FOWQ01000001; SFO73649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5JLS6; -.
DR STRING; 1523247.SAMN05660464_0848; -.
DR OrthoDB; 9807606at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000198857; Unassembled WGS sequence.
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 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};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01934};
KW Reference proteome {ECO:0000313|Proteomes:UP000198857}.
FT BINDING 81
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 112..116
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 144
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 256
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 81
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
SQ SEQUENCE 265 AA; 29569 MW; A907030771D45AE1 CRC64;
MKPEEFTDIR YEVEEDDHAV ITIDRQERMN SFRGRTVDEL ISAFKHAWAD HRVGSVILTA
AGERAFCTGG DVKERAETGG YGETEWGTFE IERLHRIIRD IPKPVIAAVN GIAIGGGHVL
HVLCDLTVAC EEATFAQAGP RVGSFDAGFG SAYLARVVGE KRARQIWFLL DRYDAATAER
WGLVNAVVPR DQLLDTAREW ARRIGSYSPT ALRFLKHSFN ADSDHLSGIS HLAFDGLAQF
AVSEEGMEGA QAFAEKRQPD FRRFR
//
