MENB_HAEIN
ID MENB_HAEIN Reviewed; 285 AA.
AC P44960;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01934};
DE Short=DHNA-CoA synthase {ECO:0000255|HAMAP-Rule:MF_01934};
DE EC=4.1.3.36 {ECO:0000255|HAMAP-Rule:MF_01934};
GN Name=menB {ECO:0000255|HAMAP-Rule:MF_01934}; OrderedLocusNames=HI_0968;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-
CC naphthoyl-CoA (DHNA-CoA). {ECO:0000255|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:0000255|HAMAP-Rule:MF_01934};
CC -!- COFACTOR:
CC Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544;
CC Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_01934}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01934}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01934}.
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DR EMBL; L42023; AAC22625.1; -; Genomic_DNA.
DR PIR; B64105; B64105.
DR RefSeq; NP_439129.1; NC_000907.1.
DR RefSeq; WP_005693314.1; NC_000907.1.
DR AlphaFoldDB; P44960; -.
DR SMR; P44960; -.
DR STRING; 71421.HI_0968; -.
DR EnsemblBacteria; AAC22625; AAC22625; HI_0968.
DR KEGG; hin:HI_0968; -.
DR PATRIC; fig|71421.8.peg.1009; -.
DR eggNOG; COG0447; Bacteria.
DR HOGENOM; CLU_009834_7_7_6; -.
DR OMA; IFKQTDA; -.
DR PhylomeDB; P44960; -.
DR BioCyc; HINF71421:G1GJ1-1009-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.12.10; -; 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; PTHR43113; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR01929; menB; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Lyase; Menaquinone biosynthesis; Reference proteome.
FT CHAIN 1..285
FT /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT /id="PRO_0000109327"
FT BINDING 45
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 84..88
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 97
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 129..133
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 154..156
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 155
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 161
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 258
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 273
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 97
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 258
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
SQ SEQUENCE 285 AA; 31700 MW; 4A2F68CF0DCEC996 CRC64;
MQNPKDDVLY APVEWIDHSE GYSDIRYHKS TDGIAKITIN RPEVRNAFRP QTVKEMMTAF
SDARFDENIG VIVLTGEGEK AFCSGGDQKV RGDYGGYKDD SGVHHLNVLD FQRDIRSCPK
PVVAMVAGYA IGGGHVLHML CDLTIAAENA IFGQTGPKVG SFDGGWGASY MARLVGQKKA
REIWFLCRQY NAQEALDMGL VNTVVPYADL EKETVRWCRE MLRNSPIAIR CLKAALNADC
DGQAGLQELA GNATMLFYMT EEGQEGRNAF NEKRAPDFSK FRRNP
