MENB_ARATH
ID MENB_ARATH Reviewed; 337 AA.
AC Q8GYN9; B3LF97; O22696;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal;
DE Short=DHNS;
DE EC=4.1.3.36;
DE AltName: Full=Enoyl-CoA hydratase/isomerase D;
DE Short=ECHID;
DE AltName: Full=Naphthoate synthase;
GN Name=MENB; OrderedLocusNames=At1g60550; ORFNames=F8A5.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-20.
RX PubMed=20150517; DOI=10.1093/jxb/erq014;
RA Babujee L., Wurtz V., Ma C., Lueder F., Soni P., van Dorsselaer A.,
RA Reumann S.;
RT "The proteome map of spinach leaf peroxisomes indicates partial
RT compartmentalization of phylloquinone (vitamin K1) biosynthesis in plant
RT peroxisomes.";
RL J. Exp. Bot. 61:1441-1453(2010).
CC -!- FUNCTION: Involved in the biosynthesis of phylloquinone (vitamin K1).
CC Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-
CC CoA (DHNA-CoA) (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=hydrogencarbonate; Xref=ChEBI:CHEBI:17544; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:20150517,
CC ECO:0000305|PubMed:17951448}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. MenB
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71952.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002292; AAB71952.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33696.1; -; Genomic_DNA.
DR EMBL; AK117477; BAC42141.1; -; mRNA.
DR EMBL; BT033085; ACF04808.1; -; mRNA.
DR PIR; G96630; G96630.
DR RefSeq; NP_176255.2; NM_104739.5.
DR AlphaFoldDB; Q8GYN9; -.
DR SMR; Q8GYN9; -.
DR STRING; 3702.AT1G60550.1; -.
DR iPTMnet; Q8GYN9; -.
DR PaxDb; Q8GYN9; -.
DR PRIDE; Q8GYN9; -.
DR ProteomicsDB; 250625; -.
DR EnsemblPlants; AT1G60550.1; AT1G60550.1; AT1G60550.
DR GeneID; 842350; -.
DR Gramene; AT1G60550.1; AT1G60550.1; AT1G60550.
DR KEGG; ath:AT1G60550; -.
DR Araport; AT1G60550; -.
DR TAIR; locus:2036626; AT1G60550.
DR eggNOG; KOG1680; Eukaryota.
DR HOGENOM; CLU_009834_7_7_1; -.
DR InParanoid; Q8GYN9; -.
DR OMA; IFKQTDA; -.
DR OrthoDB; 1221604at2759; -.
DR PhylomeDB; Q8GYN9; -.
DR PRO; PR:Q8GYN9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GYN9; baseline and differential.
DR Genevisible; Q8GYN9; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IBA:GO_Central.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; TAS: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; 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 Isomerase; Lyase; Peroxisome; Reference proteome.
FT CHAIN 1..337
FT /note="1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal"
FT /id="PRO_0000406985"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137..141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181..185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 206..208
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 215
FT /note="Important for catalysis"
FT /evidence="ECO:0000255"
FT SITE 310
FT /note="Important for catalysis"
FT /evidence="ECO:0000255"
FT MUTAGEN 20
FT /note="H->V: Loss of peroxisomal targeting."
FT /evidence="ECO:0000269|PubMed:20150517"
FT CONFLICT 228
FT /note="G -> C (in Ref. 3; BAC42141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37056 MW; DCC1E02D8108F4EA CRC64;
MADSNELGSA SRRLSVVTNH LIPIGFSPAR ADSVELCSAS SMDDRFHKVH GEVPTHEVVW
KKTDFFGEGD NKEFVDIIYE KALDEGIAKI TINRPERRNA FRPQTVKELM RAFNDARDDS
SVGVIILTGK GTKAFCSGGD QALRTQDGYA DPNDVGRLNV LDLQVQIRRL PKPVIAMVAG
YAVGGGHILH MVCDLTIAAD NAIFGQTGPK VGSFDAGYGS SIMSRLVGPK KAREMWFMTR
FYTASEAEKM GLINTVVPLE DLEKETVKWC REILRNSPTA IRVLKAALNA VDDGHAGLQG
LGGDATLLFY GTEEATEGRT AYMHRRPPDF SKFHRRP
