MENB_STAAC
ID MENB_STAAC Reviewed; 273 AA.
AC Q5HH38;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SACOL1054;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=20643650; DOI=10.1074/jbc.m110.147702;
RA Jiang M., Chen M., Guo Z.F., Guo Z.;
RT "A bicarbonate cofactor modulates 1,4-dihydroxy-2-naphthoyl-coenzyme a
RT synthase in menaquinone biosynthesis of Escherichia coli.";
RL J. Biol. Chem. 285:30159-30169(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE ANALOG
RP ACETOACETYL-COA, AND SUBUNIT.
RX PubMed=18007038; DOI=10.1107/s1744309107047720;
RA Ulaganathan V., Agacan M.F., Buetow L., Tulloch L.B., Hunter W.N.;
RT "Structure of Staphylococcus aureus1,4-dihydroxy-2-naphthoyl-CoA synthase
RT (MenB) in complex with acetoacetyl-CoA.";
RL Acta Crystallogr. F 63:908-913(2007).
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 ECO:0000269|PubMed:20643650};
CC -!- COFACTOR:
CC Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01934,
CC ECO:0000269|PubMed:20643650};
CC Note=The hydrogencarbonate anion plays the same catalytic role (proton
CC acceptor) as the side-chain carboxylate group of the essential 'Asp-
CC 185' found in actinobacteria, archaea, bacteroidetes, and
CC deltaproteobacteria. {ECO:0000269|PubMed:20643650};
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: Homodimer. Can also form trimers and higher oligomers.
CC {ECO:0000269|PubMed:18007038}.
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; CP000046; AAW36519.1; -; Genomic_DNA.
DR RefSeq; WP_000184947.1; NC_002951.2.
DR PDB; 2UZF; X-ray; 2.90 A; A/B=1-273.
DR PDBsum; 2UZF; -.
DR AlphaFoldDB; Q5HH38; -.
DR SMR; Q5HH38; -.
DR EnsemblBacteria; AAW36519; AAW36519; SACOL1054.
DR KEGG; sac:SACOL1054; -.
DR HOGENOM; CLU_009834_7_7_9; -.
DR OMA; IFKQTDA; -.
DR BRENDA; 4.1.3.36; 3352.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR EvolutionaryTrace; Q5HH38; -.
DR Proteomes; UP000000530; Chromosome.
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 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Menaquinone biosynthesis.
FT CHAIN 1..273
FT /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT /id="PRO_0000224814"
FT REGION 254..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
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 ECO:0000269|PubMed:18007038"
FT BINDING 73..77
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 ECO:0000269|PubMed:18007038"
FT BINDING 85
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 117..121
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 142..144
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT BINDING 143
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 149
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 ECO:0000269|PubMed:18007038"
FT BINDING 246
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 261
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 85
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT SITE 246
FT /note="Important for catalysis"
FT /evidence="ECO:0000250|UniProtKB:P0ABU0, ECO:0000255|HAMAP-
FT Rule:MF_01934"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 60..72
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2UZF"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 214..228
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 230..246
FT /evidence="ECO:0007829|PDB:2UZF"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:2UZF"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:2UZF"
SQ SEQUENCE 273 AA; 30426 MW; DFB230B838E559FB CRC64;
MTNRQWETLR EYDEIKYEFY EGIAKVTINR PEVRNAFTPK TVAEMIDAFS RARDDQNVSV
IVLTGEGDLA FCSGGDQKKR GHGGYVGEDQ IPRLNVLDLQ RLIRIIPKPV IAMVKGYAVG
GGNVLNVVCD LTIAADNAIF GQTGPKVGSF DAGYGSGYLA RIVGHKKARE IWYLCRQYNA
QEALDMGLVN TVVPLEKVED ETVQWCKEIM KHSPTALRFL KAAMNADTDG LAGLQQMAGD
ATLLYYTTDE AKEGRDAFKE KRDPDFDQFP KFP
