ID A0A1X1RML1_MYCCE Unreviewed; 300 AA.
AC A0A1X1RML1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AWB95_16680 {ECO:0000313|EMBL:ORV09863.1}, CQY23_07090
GN {ECO:0000313|EMBL:PIB79672.1};
OS Mycobacterium celatum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=28045 {ECO:0000313|EMBL:ORV09863.1, ECO:0000313|Proteomes:UP000193907};
RN [1] {ECO:0000313|EMBL:ORV09863.1, ECO:0000313|Proteomes:UP000193907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44243 {ECO:0000313|EMBL:ORV09863.1,
RC ECO:0000313|Proteomes:UP000193907};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PIB79672.1, ECO:0000313|Proteomes:UP000230971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 12882 {ECO:0000313|EMBL:PIB79672.1,
RC ECO:0000313|Proteomes:UP000230971};
RX PubMed=29030295; DOI=10.1016/j.meegid.2017.10.013;
RA Tortoli E., Fedrizzi T., Meehan C.J., Trovato A., Grottola A.,
RA Giacobazzi E., Serpini G.F., Tagliazucchi S., Fabio A., Bettua C.,
RA Bertorelli R., Frascaro F., De Sanctis V., Pecorari M., Jousson O.,
RA Segata N., Cirillo D.M.;
RT "The new phylogeny of the genus Mycobacterium: The old and the news.";
RL Infect. Genet. Evol. 56:19-25(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORV09863.1}.
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DR EMBL; LQOM01000037; ORV09863.1; -; Genomic_DNA.
DR EMBL; PDKV01000006; PIB79672.1; -; Genomic_DNA.
DR RefSeq; WP_062538282.1; NZ_PDKV01000006.1.
DR STRING; 28045.AWB95_16680; -.
DR OrthoDB; 9807606at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000193907; Unassembled WGS sequence.
DR Proteomes; UP000230971; 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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01934, ECO:0000313|EMBL:PIB79672.1};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01934}.
FT BINDING 44
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 89..93
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 101
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 143..147
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 170
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 176
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 273
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 288
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 101
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 171
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 273
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
SQ SEQUENCE 300 AA; 33230 MW; 700C5D450930A849 CRC64;
MSDNPFDADA WRPVDGFAGL TDITYHRHVT DATVRVAFNR PEVRNAFRPQ TVDELYRALD
HARMSPDVGV ILLTGNGPSP RDGGWAFCSG GDQRIRGRTG YQYASGETAD TVDAARAGRL
HILEVQRLIR FMPKVVICLV SGWAAGGGHS LHVVCDLTLA SRQHARFKQT DADVGSFDGG
YGSAYLARQV GQKFAREIFF LGREYTAEQM HEMGAVNAVV DHAELEAAGI QWAAEINAKS
PQAQRMLKYA FNLLDDGLVG QQLFAGEATR LAYMTDEAVE GRDAFLEKRP PDWSRFPRYF
//
