ID W2UPC7_9FLAO Unreviewed; 279 AA.
AC W2UPC7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=P278_10480 {ECO:0000313|EMBL:ETN95326.1};
OS Zhouia amylolytica AD3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zhouia.
OX NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN95326.1, ECO:0000313|Proteomes:UP000018850};
RN [1] {ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850};
RA Jin H., Jeon C.O.;
RT "Draft genome sequence from a member of Zhouia, isolated tidal flat.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN95326.1, ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|EMBL:ETN95326.1,
RC ECO:0000313|Proteomes:UP000018850};
RX PubMed=27151796;
RA Jia B., Jin H.M., Lee H.J., Jeon C.O.;
RT "Draft Genome Sequence of Zhouia amylolytica AD3, Isolated from Tidal Flat
RT Sediment.";
RL Genome Announc. 4:0-0(2016).
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:ETN95326.1}.
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DR EMBL; AYXY01000019; ETN95326.1; -; Genomic_DNA.
DR RefSeq; WP_038263361.1; NZ_AYXY01000019.1.
DR AlphaFoldDB; W2UPC7; -.
DR STRING; 376730.SAMN04487906_2426; -.
DR PATRIC; fig|1286632.3.peg.1043; -.
DR eggNOG; COG0447; Bacteria.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000018850; 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:UP000018850}.
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 150
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 156
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 253
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT BINDING 268
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 151
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
FT SITE 253
FT /note="Important for catalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01934"
SQ SEQUENCE 279 AA; 31046 MW; 3EF6F0A86AB25141 CRC64;
MSSPNWRIIE GYEDITYKKC DGVARIAFNR PNVRNAFRPK TTAELYKAFY DANEDTSIGV
VLLSAEGPST KDGVWSFCSG GDQKARGKQG YVGDDGYHRL NILEVQRLIR FMPKAVIAVV
PGWAVGGGHS LHVVCDLTLA SKEHAIFKQT DADVTSFDGG YGSAYLAKMV GQKKAREIFF
LGRNYSAQEA YEMGMVNAVI PHDELESTAY EWAQEILAKS PISIKMLKFA MNLTDDGMVG
QQVFAGEATR LAYMTDEAKE GRNAFLEKRK PNFDKKWIP
//