MENA_ARATH
ID MENA_ARATH Reviewed; 382 AA.
AC Q0WUA3; Q6NLY2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic;
DE EC=2.5.1.130 {ECO:0000269|PubMed:15686525};
DE AltName: Full=1,4-dihydroxy-2-naphthoate phytyltransferase;
DE AltName: Full=1,4-dihydroxy-2-naphthoate polyprenyltransferase;
DE AltName: Full=Protein ABERRANT CHLOROPLAST DEVELOPMENT 4;
DE AltName: Full=menA-like protein;
DE Short=AtMENA;
DE Flags: Precursor;
GN Name=ABC4; OrderedLocusNames=At1g60600; ORFNames=F8A5.36;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE (ISOFORM 1).
RX PubMed=15686525; DOI=10.1111/j.1365-313x.2004.02326.x;
RA Shimada H., Ohno R., Shibata M., Ikegami I., Onai K., Ohto M.A.,
RA Takamiya K.;
RT "Inactivation and deficiency of core proteins of photosystems I and II
RT caused by genetical phylloquinone and plastoquinone deficiency but retained
RT lamellar structure in a T-DNA mutant of Arabidopsis.";
RL Plant J. 41:627-637(2005).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Cheuk R., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the synthesis of phylloquinone (vitamin K1).
CC Catalyzes the transfer of a prenyl chain to 2-carboxy-1,4-
CC naphthoquinone. {ECO:0000269|PubMed:15686525}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4-dioxo-2-naphthoate + H(+) + phytyl diphosphate = CO2 +
CC demethylphylloquinone + diphosphate; Xref=Rhea:RHEA:47740,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:31087,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:75434, ChEBI:CHEBI:87842;
CC EC=2.5.1.130; Evidence={ECO:0000269|PubMed:15686525};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:15686525}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15686525}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0WUA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WUA3-2; Sequence=VSP_040861;
CC -!- DISRUPTION PHENOTYPE: Slower growth and dwarfism. Albino phenotype in
CC aging leaves. Decreased number of chloroplasts, but normal lamellar
CC structure retained. Absence of phylloquinone and 97% decrease in the
CC content of plastoquinone.
CC -!- SIMILARITY: Belongs to the MenA family. Type 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AC002292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE33701.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33702.1; -; Genomic_DNA.
DR EMBL; BT012196; AAS76683.1; -; mRNA.
DR EMBL; AK227267; BAE99295.1; -; mRNA.
DR RefSeq; NP_001117518.1; NM_001124046.2. [Q0WUA3-1]
DR RefSeq; NP_176259.2; NM_104743.3. [Q0WUA3-2]
DR AlphaFoldDB; Q0WUA3; -.
DR BioGRID; 27578; 15.
DR IntAct; Q0WUA3; 3.
DR STRING; 3702.AT1G60600.2; -.
DR PaxDb; Q0WUA3; -.
DR PRIDE; Q0WUA3; -.
DR ProteomicsDB; 250639; -. [Q0WUA3-1]
DR EnsemblPlants; AT1G60600.1; AT1G60600.1; AT1G60600. [Q0WUA3-2]
DR EnsemblPlants; AT1G60600.2; AT1G60600.2; AT1G60600. [Q0WUA3-1]
DR GeneID; 842354; -.
DR Gramene; AT1G60600.1; AT1G60600.1; AT1G60600. [Q0WUA3-2]
DR Gramene; AT1G60600.2; AT1G60600.2; AT1G60600. [Q0WUA3-1]
DR KEGG; ath:AT1G60600; -.
DR Araport; AT1G60600; -.
DR TAIR; locus:2036484; AT1G60600.
DR eggNOG; KOG4581; Eukaryota.
DR InParanoid; Q0WUA3; -.
DR OMA; TCGYIYQ; -.
DR OrthoDB; 1470215at2759; -.
DR PhylomeDB; Q0WUA3; -.
DR BRENDA; 2.5.1.130; 399.
DR PRO; PR:Q0WUA3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WUA3; baseline and differential.
DR Genevisible; Q0WUA3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046428; F:1,4-dihydroxy-2-naphthoate octaprenyltransferase activity; ISS:TAIR.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IMP:TAIR.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IMP:TAIR.
DR GO; GO:0010236; P:plastoquinone biosynthetic process; IMP:TAIR.
DR GO; GO:0032194; P:ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate; IBA:GO_Central.
DR GO; GO:0042371; P:vitamin K biosynthetic process; IBA:GO_Central.
DR CDD; cd13962; PT_UbiA_UBIAD1; 1.
DR HAMAP; MF_01938; MenA_2; 1.
DR InterPro; IPR011937; DHNA_phytyltransferase_MenA.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR026046; UBIAD1.
DR PANTHER; PTHR13929; PTHR13929; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR02235; menA_cyano-plnt; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Membrane; Plastid; Reference proteome;
KW Transferase; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..382
FT /note="2-carboxy-1,4-naphthoquinone phytyltransferase,
FT chloroplastic"
FT /id="PRO_0000406881"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_040861"
FT CONFLICT 126
FT /note="L -> Q (in Ref. 4; AAS76683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42037 MW; B8E51B6C43BE601B CRC64;
MVNFVSLCDI KYGFVPKNST DLFVKRKIHK LPSRGDVITR LPVFGSNARE NLNAKPRRNL
RVRPIFCKSY GDAAKVYQEE EIPRAKLIWR AIKLPMYSVA LVPLTVGASA AYLETGLFLA
RRYVTLLLSS ILIITWLNLS NDVYDFDTGA DKNKMESVVN LVGSRTGTLA AAITSLALGV
SGLVWTSLNA SNIRAILLLA SAILCGYVYQ CPPFRLSYQG LGEPLCFAAF GPFATTAFYL
LLGSSSEMRH LPLSGRVLSS SVLVGFTTSL ILFCSHFHQV DGDLAVGKYS PLVRLGTEKG
AFVVRWTIRL LYSMLLVLGL TRILPLPCTL MCFLTLPVGN LVSSYVEKHH KDNGKIFMAK
YYCVRLHALL GAALSLGLVI AR
