ID A0A0W7W846_9MICO Unreviewed; 304 AA.
AC A0A0W7W846;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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=AUL38_10885 {ECO:0000313|EMBL:KUF06758.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF06758.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF06758.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF06758.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-2015) 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}.
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:KUF06758.1}.
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DR EMBL; LOHP01000063; KUF06758.1; -; Genomic_DNA.
DR RefSeq; WP_059061511.1; NZ_LOHP01000063.1.
DR AlphaFoldDB; A0A0W7W846; -.
DR STRING; 663704.AUL38_10885; -.
DR OrthoDB; 9807606at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000053012; 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};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01934};
KW Reference proteome {ECO:0000313|Proteomes:UP000053012}.
FT BINDING 47
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 92..96
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 104
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 147..151
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 174
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 180
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 277
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 292
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 104
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 175
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 277
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
SQ SEQUENCE 304 AA; 33443 MW; A19B5F1F986ADC24 CRC64;
MTKQVSDIFD PSVWEVAPGA EGYTDITAHL SLDGRIARIA VERPEVRNAF RPHTVDELFD
ALDRVRVNPK VGVVLLTGNG PSQKDGGWAF CSGGDQRIRG RDGYKYSDSE TAVGPEALAR
AGRLHILEVQ RLIRFMPKVV IALVPGWAAG GGHSLNVVCD LTIASREHAK FKQTDADVGS
FDAGYGSAYF AKQVGQKNAR EIFFLAREYD AERAREIGAV NEVVPHAELE STGIEWAREI
LGKSPTAIRM LKYAMNAVDD GIVGQQLFAG ETTRLAYGTD EAVEGRDSFL EKRDPDWSPF
PYHY
//
