MENE_ARATH
ID MENE_ARATH Reviewed; 560 AA.
AC Q8VYJ1; Q9S9P7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=2-succinylbenzoate--CoA ligase, chloroplastic/peroxisomal;
DE EC=6.2.1.26;
DE AltName: Full=Acyl-activating enzyme 14;
DE AltName: Full=O-succinylbenzoyl-CoA ligase;
DE Flags: Precursor;
GN Name=AAE14; Synonyms=MENE; OrderedLocusNames=At1g30520;
GN ORFNames=F26G16.14, F26G16.3;
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], TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18208520; DOI=10.1111/j.1365-313x.2008.03416.x;
RA Kim H.U., van Oostende C., Basset G.J., Browse J.;
RT "The AAE14 gene encodes the Arabidopsis o-succinylbenzoyl-CoA ligase that
RT is essential for phylloquinone synthesis and photosystem-I function.";
RL Plant J. 54:272-283(2008).
RN [6]
RP SUBCELLULAR LOCATION.
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 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
CC {ECO:0000269|PubMed:18208520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-succinylbenzoate + ATP + CoA = 2-succinylbenzoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:17009, ChEBI:CHEBI:18325,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57364, ChEBI:CHEBI:456215; EC=6.2.1.26;
CC Evidence={ECO:0000269|PubMed:18208520};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass
CC membrane protein. Peroxisome membrane; Multi-pass membrane protein.
CC Note=Accumulates in discrete foci within the chloroplast.
CC -!- TISSUE SPECIFICITY: High expression in young leaves and flowers. Not
CC expressed in roots. {ECO:0000269|PubMed:12805634,
CC ECO:0000269|PubMed:18208520}.
CC -!- DISRUPTION PHENOTYPE: Lack of phylloquinone and seedling lethal.
CC {ECO:0000269|PubMed:18208520}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC MenE subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19755.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY250843; AAP03026.1; -; mRNA.
DR EMBL; AC009917; AAF19755.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31239.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60008.1; -; Genomic_DNA.
DR EMBL; AY070739; AAL50080.1; -; mRNA.
DR EMBL; BT010462; AAQ65085.1; -; mRNA.
DR PIR; C86430; C86430.
DR RefSeq; NP_001322322.1; NM_001332903.1.
DR RefSeq; NP_174340.2; NM_102789.5.
DR AlphaFoldDB; Q8VYJ1; -.
DR SMR; Q8VYJ1; -.
DR STRING; 3702.AT1G30520.1; -.
DR PaxDb; Q8VYJ1; -.
DR PRIDE; Q8VYJ1; -.
DR ProteomicsDB; 238952; -.
DR EnsemblPlants; AT1G30520.1; AT1G30520.1; AT1G30520.
DR EnsemblPlants; AT1G30520.2; AT1G30520.2; AT1G30520.
DR GeneID; 839932; -.
DR Gramene; AT1G30520.1; AT1G30520.1; AT1G30520.
DR Gramene; AT1G30520.2; AT1G30520.2; AT1G30520.
DR KEGG; ath:AT1G30520; -.
DR Araport; AT1G30520; -.
DR TAIR; locus:2028165; AT1G30520.
DR eggNOG; KOG1177; Eukaryota.
DR HOGENOM; CLU_000022_59_7_1; -.
DR InParanoid; Q8VYJ1; -.
DR OMA; ACHVFIP; -.
DR OrthoDB; 386992at2759; -.
DR PhylomeDB; Q8VYJ1; -.
DR BioCyc; ARA:AT1G30520-MON; -.
DR BRENDA; 6.2.1.26; 399.
DR PRO; PR:Q8VYJ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYJ1; baseline and differential.
DR Genevisible; Q8VYJ1; 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:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0008756; F:o-succinylbenzoate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IMP:TAIR.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Ligase; Membrane; Nucleotide-binding; Peroxisome;
KW Plastid; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..15
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 16..560
FT /note="2-succinylbenzoate--CoA ligase,
FT chloroplastic/peroxisomal"
FT /id="PRO_0000406984"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 558..560
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 560 AA; 61917 MW; 4EBFB5A503C1914A CRC64;
MANHSRPHIC QCLTRLASVK RNAVVTVYGN RKRTGREFVD GVLSLAAGLI RLGLRNGDVV
SIAAFNSDLF LEWLLAVALV GGVVAPLNYR WSLKEAKMAM LLVEPVLLVT DETCVSWCID
VQNGDIPSLK WRVLMESTST DFANELNQFL TTEMLKQRTL VPSLATYAWA SDDAVVICFT
SGTTGRPKGV TISHLAFITQ SLAKIAIAGY GEDDVYLHTS PLVHIGGLSS AMAMLMVGAC
HVLLPKFDAK TALQVMEQNH ITCFITVPAM MADLIRVNRT TKNGAENRGV RKILNGGGSL
SSELLKEAVN IFPCARILSA YGMTEACSSL TFMTLHDPTQ ESFKVTYPLL NQPKQGTCVG
KPAPHIELMV KLDEDSSRVG KILTRGPHTM LRYWGHQVAQ ENVETSESRS NEAWLDTGDI
GAFDEFGNLW LIGRSNGRIK TGGENVYPEE VEAVLVEHPG IVSAVVIGVI DTRLGEMVVA
CVRLQEKWIW SDVENRKGSF QLSSETLKHH CRTQNLTGFK IPKRFVRWEK QFPLTTTGKV
KRDEVRRQVL SHFQIMTSSL
