MENB_SALTY
ID MENB_SALTY Reviewed; 285 AA.
AC Q7CQ56;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=STM2307;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HYDROGENCARBONATE
RP ION, AND SUBUNIT.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RA Minasov G., Wawrzak Z., Skarina T., Onopriyenko O., Peterson S.N.,
RA Savchenko A., Anderson W.F.;
RT "2.15 angstrom resolution crystal structure of naphthoate synthase from
RT Salmonella typhimurium.";
RL Submitted (OCT-2009) 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: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 -!- SUBUNIT: Homohexamer. {ECO:0000269|Ref.2}.
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; AE006468; AAL21208.1; -; Genomic_DNA.
DR RefSeq; NP_461249.1; NC_003197.2.
DR RefSeq; WP_000640013.1; NC_003197.2.
DR PDB; 3H02; X-ray; 2.15 A; A/B/C/D/E/F=1-285.
DR PDBsum; 3H02; -.
DR AlphaFoldDB; Q7CQ56; -.
DR SMR; Q7CQ56; -.
DR STRING; 99287.STM2307; -.
DR PaxDb; Q7CQ56; -.
DR EnsemblBacteria; AAL21208; AAL21208; STM2307.
DR GeneID; 1253829; -.
DR KEGG; stm:STM2307; -.
DR PATRIC; fig|99287.12.peg.2442; -.
DR HOGENOM; CLU_009834_7_7_6; -.
DR OMA; IFKQTDA; -.
DR PhylomeDB; Q7CQ56; -.
DR BioCyc; SENT99287:STM2307-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR EvolutionaryTrace; Q7CQ56; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Lyase; Menaquinone biosynthesis; Reference proteome.
FT CHAIN 1..285
FT /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT /id="PRO_0000403188"
FT BINDING 45
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT 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 ECO:0000269|Ref.2"
FT BINDING 155
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT 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:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT BINDING 258
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT BINDING 273
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT SITE 97
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT SITE 258
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 71..83
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:3H02"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:3H02"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:3H02"
SQ SEQUENCE 285 AA; 31693 MW; 9A1F2D16742A975A CRC64;
MIYPDETMLY APVEWHDCSE GYTDIRYEKS TDGIAKITIN RPQVRNAFRP LTVKEMIQAL
ADARYDDNVG VIILTGEGDK AFCAGGDQKV RGDYGGYQDD SGVHHLNVLD FQRQIRTCPK
PVVAMVAGYS IGGGHVLHMM CDLTIAAENA IFGQTGPKVG SFDGGWGASY MARIVGQKKA
REIWFLCRQY DAQQALDMGL VNTVVPLADL EKETVRWCRE MLQNSPMALR CLKAALNADC
DGQAGLQELA GNATMLFYMT EEGQEGRNAF NQKRQPDFSK FKRNP
