MENB_STAAM
ID MENB_STAAM Reviewed; 273 AA.
AC Q99V48;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=SAV1045;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB57207.1; -; Genomic_DNA.
DR RefSeq; WP_000184945.1; NC_002758.2.
DR AlphaFoldDB; Q99V48; -.
DR SMR; Q99V48; -.
DR World-2DPAGE; 0002:Q99V48; -.
DR PaxDb; Q99V48; -.
DR EnsemblBacteria; BAB57207; BAB57207; SAV1045.
DR KEGG; sav:SAV1045; -.
DR HOGENOM; CLU_009834_7_7_9; -.
DR OMA; IFKQTDA; -.
DR PhylomeDB; Q99V48; -.
DR BioCyc; SAUR158878:SAV_RS05640-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000002481; 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 3: Inferred from homology;
KW Lyase; Menaquinone biosynthesis.
FT CHAIN 1..273
FT /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT /id="PRO_0000224815"
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 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 BINDING 85
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 117..121
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 142..144
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000255|HAMAP-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:0000255|HAMAP-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 BINDING 246
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 261
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 85
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 246
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
SQ SEQUENCE 273 AA; 30412 MW; DE689BC838E41DBE CRC64;
MTNRQWETLR EYDEIKYEFY EGIAKVTINR PEVRNAFTPK TVAEMIDAFS RARDDQNVSV
IVLTGEGDLA FCSGGDQKKR GHGGYVGEDQ IPRLNVLDLQ RLIRIIPKPV IAMVKGYAVG
GGNVLNVVCD LTIAADNAIF GQTGPKVGSF DAGYGSGYLA RIVGHKKARE IWYLCRQYNA
QEALDMGLVN TVVPLDKVED ETVQWCKEIM KHSPTALRFL KAAMNADTDG LAGLQQMAGD
ATLLYYTTDE AKEGRDAFKE KRDPDFDQFP KFP
