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Database: UniProt
Entry: A0A1H9FKG0_9FLAO
LinkDB: A0A1H9FKG0_9FLAO
Original site: A0A1H9FKG0_9FLAO 
ID   A0A1H9FKG0_9FLAO        Unreviewed;       279 AA.
AC   A0A1H9FKG0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05421824_1503 {ECO:0000313|EMBL:SEQ38427.1};
OS   Hyunsoonleella jejuensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=419940 {ECO:0000313|EMBL:SEQ38427.1, ECO:0000313|Proteomes:UP000198999};
RN   [1] {ECO:0000313|EMBL:SEQ38427.1, ECO:0000313|Proteomes:UP000198999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21035 {ECO:0000313|EMBL:SEQ38427.1,
RC   ECO:0000313|Proteomes:UP000198999};
RA   de Groot N.N.;
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; FOFN01000002; SEQ38427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9FKG0; -.
DR   STRING; 419940.SAMN05421824_1503; -.
DR   OrthoDB; 9775794at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00167.
DR   Proteomes; UP000198999; 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:UP000198999}.
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;  31061 MW;  4CA6B199541A9782 CRC64;
     MITPEWITVK EYEDITYKKS DGVARIAFNR PNVRNAFRPK TTSELYDAFY DANEDTSIGV
     VLLSAEGPST KDGVYSFCSG GDQKARGHQG YVGEDGYHRL NILEVQRLIR FMPKAVIAVV
     PGWAVGGGHS LHVVCDLTLA SKEHAIFKQT DADVTSFDGG YGSAYLAKMV GQKKAREIFF
     LGRNYSAQEA FEMGMVNAVI PHDKLESTAY EWAQEILAKS PTSIKMLKFA MNLTDDGMVG
     QQVFAGEATR LAYMTDEAKE GRDAFLEKRK PNFNKKWIP
//
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