MENB_BACSU
ID MENB_BACSU Reviewed; 271 AA.
AC P23966; O34567;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 152.
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=BSU30800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / RB1;
RX PubMed=1629163; DOI=10.1128/jb.174.15.5063-5071.1992;
RA Driscoll J.R., Taber H.W.;
RT "Sequence organization and regulation of the Bacillus subtilis menBE
RT operon.";
RL J. Bacteriol. 174:5063-5071(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN MENAQUINONE
RP BIOSYNTHESIS.
RC STRAIN=168 / RB1;
RX PubMed=8566759; DOI=10.1016/0378-1119(95)00662-1;
RA Rowland B., Hill K., Miller P., Driscoll J.R., Taber H.W.;
RT "Structural organization of a Bacillus subtilis operon encoding menaquinone
RT biosynthetic enzymes.";
RL Gene 167:105-109(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP FUNCTION AS A DHNA-COA SYNTHASE, 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).
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 ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:8566759}.
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 -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01934}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50401.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC37016.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M74521; AAA50401.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M74538; AAC37016.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF008220; AAC00226.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15058.1; -; Genomic_DNA.
DR PIR; F69656; F69656.
DR RefSeq; NP_390958.1; NC_000964.3.
DR RefSeq; WP_003229054.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P23966; -.
DR SMR; P23966; -.
DR STRING; 224308.BSU30800; -.
DR jPOST; P23966; -.
DR PaxDb; P23966; -.
DR PRIDE; P23966; -.
DR EnsemblBacteria; CAB15058; CAB15058; BSU_30800.
DR GeneID; 937195; -.
DR KEGG; bsu:BSU30800; -.
DR PATRIC; fig|224308.179.peg.3338; -.
DR eggNOG; COG0447; Bacteria.
DR InParanoid; P23966; -.
DR OMA; IFKQTDA; -.
DR PhylomeDB; P23966; -.
DR BioCyc; BSUB:BSU30800-MON; -.
DR BioCyc; MetaCyc:MON-13812; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IDA:UniProtKB.
DR GO; GO:0071890; F:bicarbonate binding; IDA:UniProtKB.
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 Lyase; Menaquinone biosynthesis; Reference proteome.
FT CHAIN 1..271
FT /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT /id="PRO_0000109324"
FT REGION 250..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71..75
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 83
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 115..119
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 140..142
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 141
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 147
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 244
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 259
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 83
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 244
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT CONFLICT 13
FT /note="I -> D (in Ref. 1; AAA50401 and 2; AAC37016)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 29899 MW; D7D74C84E35A87B0 CRC64;
MAEWKTKRTY DEILYETYNG IAKITINRPE VHNAFTPKTV AEMIDAFADA RDDQNVGVIV
LAGAGDKAFC SGGDQKVRGH GGYVGDDQIP RLNVLDLQRL IRVIPKPVVA MVSGYAIGGG
HVLHIVCDLT IAADNAIFGQ TGPKVGSFDA GYGSGYLARI VGHKKAREIW YLCRQYNAQE
ALDMGLVNTV VPLEQLEEET IKWCEEMLEK SPTALRFLKA AFNADTDGLA GIQQFAGDAT
LLYYTTDEAK EGRDSFKEKR KPDFGQFPRF P
