MENB_MYCS2
ID MENB_MYCS2 Reviewed; 309 AA.
AC A0QRD3; I7FXI8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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};
GN OrderedLocusNames=MSMEG_1075, MSMEI_1042;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION AS A DHNA-COA SYNTHASE, CATALYTIC ACTIVITY, AND SITE ASP-180.
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}.
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 -!- 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; CP000480; ABK74961.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37522.1; -; Genomic_DNA.
DR RefSeq; WP_003892442.1; NZ_SIJM01000011.1.
DR RefSeq; YP_885471.1; NC_008596.1.
DR AlphaFoldDB; A0QRD3; -.
DR SMR; A0QRD3; -.
DR STRING; 246196.MSMEI_1042; -.
DR EnsemblBacteria; ABK74961; ABK74961; MSMEG_1075.
DR EnsemblBacteria; AFP37522; AFP37522; MSMEI_1042.
DR GeneID; 66732538; -.
DR KEGG; msg:MSMEI_1042; -.
DR KEGG; msm:MSMEG_1075; -.
DR PATRIC; fig|246196.19.peg.1062; -.
DR eggNOG; COG0447; Bacteria.
DR OMA; HAKRQTD; -.
DR OrthoDB; 1275789at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00167.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IDA:UniProtKB.
DR GO; GO:0009234; P:menaquinone biosynthetic process; ISS:UniProtKB.
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 Lyase; Menaquinone biosynthesis; Reference proteome.
FT CHAIN 1..309
FT /note="1,4-dihydroxy-2-naphthoyl-CoA synthase"
FT /id="PRO_0000403187"
FT BINDING 53
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 98..102
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 110
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 152..156
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 179
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 185
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 282
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT BINDING 297
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 110
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 180
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
FT SITE 282
FT /note="Important for catalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01934"
SQ SEQUENCE 309 AA; 34303 MW; CACC8113C74964B2 CRC64;
MSSQAASDNP FDPAMWERVP GFDDLTDITY HRHVLDGARQ PTVRVAFDRP EVRNAFRPHT
VDELYRVLDH ARMSSDVGVI LLTGNGPSPK DGGWAFCSGG DQRIRGRTGY QYASGETAET
VDPARAGRLH ILEVQRLIRF MPKVVICLVN GWAAGGGHSL HVTCDLTLAS REHARFKQTD
ADVGSFDGGF GSAYLARQTG QKFAREIFFL GRAYDAQTMH QMGAVNEVVD HADLEKAGLQ
YAAEINGKSP QAIRMLKFAF NLIDDGLVGQ QVFAGEATRL AYMTDEAVEG RDAFLEKRDP
DWSRFPRYF
