LIP2M_ARATH
ID LIP2M_ARATH Reviewed; 235 AA.
AC Q9SXP7; O23021;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Octanoyltransferase LIP2, mitochondrial {ECO:0000305};
DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:11427685};
DE AltName: Full=Lipoate biosynthesis protein {ECO:0000305};
DE AltName: Full=Lipoate-protein ligase {ECO:0000305};
DE AltName: Full=Lipoyl ligase {ECO:0000305};
DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000305};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000305};
DE Flags: Precursor;
GN Name=LIP2 {ECO:0000303|PubMed:11427685};
GN OrderedLocusNames=At1g04640 {ECO:0000312|Araport:AT1G04640};
GN ORFNames=T1G11.11 {ECO:0000312|EMBL:AAB80636.1};
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, AND TISSUE
RP SPECIFICITY.
RX PubMed=11427685; DOI=10.1093/pcp/pce081;
RA Wada M., Yasuno R., Jordan S.W., Cronan J.E. Jr., Wada H.;
RT "Lipoic acid metabolism in Arabidopsis thaliana: cloning and
RT characterization of a cDNA encoding lipoyltransferase.";
RL Plant Cell Physiol. 42:650-656(2001).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24872381; DOI=10.1104/pp.114.238311;
RA Ewald R., Hoffmann C., Florian A., Neuhaus E., Fernie A.R., Bauwe H.;
RT "Lipoate-protein ligase and octanoyltransferase are essential for protein
RT lipoylation in mitochondria of Arabidopsis.";
RL Plant Physiol. 165:978-990(2014).
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC octanoyl-ACP is likely to be the physiological substrate (By
CC similarity) (PubMed:11427685). Together with LIP1 is essential for
CC mitochondrial protein lipoylation during seed development. Required for
CC the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component
CC E2 proteins in leaves and roots (PubMed:24872381). {ECO:0000255|HAMAP-
CC Rule:MF_00013, ECO:0000269|PubMed:11427685,
CC ECO:0000269|PubMed:24872381}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00013,
CC ECO:0000269|PubMed:11427685};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:24872381}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (PubMed:11427685). Expressed in
CC roots, rosette leaves, cauline leaves, stems and siliques
CC (PubMed:24872381). {ECO:0000269|PubMed:11427685,
CC ECO:0000269|PubMed:24872381}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality.
CC {ECO:0000269|PubMed:24872381}.
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC acid is attached via an amide linkage to the epsilon-amino group of a
CC specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000255|HAMAP-Rule:MF_00013}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC Rule:MF_00013}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80636.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g04640 has been split into 2 genes: At1g04635 and At1g04640.; Evidence={ECO:0000305};
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DR EMBL; AB020975; BAA78386.1; -; mRNA.
DR EMBL; AC002376; AAB80636.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27726.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27727.1; -; Genomic_DNA.
DR EMBL; AF428288; AAL16120.1; -; mRNA.
DR EMBL; AY133628; AAM91458.1; -; mRNA.
DR PIR; B86179; B86179.
DR RefSeq; NP_001030961.1; NM_001035884.2.
DR RefSeq; NP_171958.1; NM_100343.3.
DR AlphaFoldDB; Q9SXP7; -.
DR SMR; Q9SXP7; -.
DR STRING; 3702.AT1G04640.2; -.
DR SwissPalm; Q9SXP7; -.
DR PaxDb; Q9SXP7; -.
DR PRIDE; Q9SXP7; -.
DR ProteomicsDB; 238659; -.
DR EnsemblPlants; AT1G04640.1; AT1G04640.1; AT1G04640.
DR EnsemblPlants; AT1G04640.2; AT1G04640.2; AT1G04640.
DR GeneID; 839462; -.
DR Gramene; AT1G04640.1; AT1G04640.1; AT1G04640.
DR Gramene; AT1G04640.2; AT1G04640.2; AT1G04640.
DR KEGG; ath:AT1G04640; -.
DR Araport; AT1G04640; -.
DR TAIR; locus:2197818; AT1G04640.
DR eggNOG; KOG0325; Eukaryota.
DR HOGENOM; CLU_035168_1_1_1; -.
DR OMA; GEVTYHC; -.
DR OrthoDB; 1491838at2759; -.
DR PhylomeDB; Q9SXP7; -.
DR BioCyc; ARA:AT1G04640-MON; -.
DR BRENDA; 2.3.1.181; 399.
DR UniPathway; UPA00538; UER00592.
DR PRO; PR:Q9SXP7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SXP7; baseline and differential.
DR Genevisible; Q9SXP7; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IDA:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00013; LipB; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..235
FT /note="Octanoyltransferase LIP2, mitochondrial"
FT /id="PRO_0000062907"
FT DOMAIN 34..218
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT ACT_SITE 178
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P60720"
FT BINDING 79..86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 147..149
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 160..162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 144
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 235 AA; 26421 MW; E0463EEFFAFE0F9F CRC64;
MRSPRTLEVW KLGTVNYLKS LKLQEKLVSE RKAHQIPDTL LSLQHPPTYT LGKRRTDHNL
LIPESELTKI GAELHYTQRG GDITFHGPHQ AILYPIISLR SIGFGARNYV ETLERSMIEF
ASIYGVKARA GNKCETGVWV GDRKIGAIGV RISSGITSHG LALNIDPDMK YFEHIVPCGI
ADKEVTSLRR ETDTLLPSEE VIHEQLVSCL AKAFSYDDVV WKEDPSLILD TQDKE
