LI2P2_ARATH
ID LI2P2_ARATH Reviewed; 280 AA.
AC P0C7R2; Q9SX89;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Octanoyltransferase LIP2p2, chloroplastic {ECO:0000305};
DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:23581459};
DE AltName: Full=Lipoate-protein ligase 2p2 {ECO:0000305};
DE AltName: Full=Lipoate-protein ligase-like protein {ECO:0000305};
DE AltName: Full=Lipoyl-[acyl-carrier-protein]-protein-N-lipoyltransferase-like protein 2p2 {ECO:0000305};
DE Flags: Precursor;
GN Name=LIP2P2 {ECO:0000303|PubMed:23581459};
GN OrderedLocusNames=At1g47578 {ECO:0000312|Araport:AT1G47578};
GN ORFNames=F16N3.14 {ECO:0000312|EMBL:AAD46029.1};
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 [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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23581459; DOI=10.1111/plb.12028;
RA Ewald R., Hoffmann C., Neuhaus E., Bauwe H.;
RT "Two redundant octanoyltransferases and one obligatory lipoyl synthase
RT provide protein-lipoylation autonomy to plastids of Arabidopsis.";
RL Plant Biol. 16:35-42(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:23581459). Together with LIP1P is essential for de
CC novo plastidial protein lipoylation during seed development. Acts
CC redundantly with LIP2P (PubMed:23581459). {ECO:0000255|HAMAP-
CC Rule:MF_00013, ECO:0000269|PubMed:23581459}.
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:23581459};
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: Plastid, chloroplast
CC {ECO:0000269|PubMed:23581459}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, cauline leaves, stems,
CC siliques and flowers. {ECO:0000269|PubMed:23581459}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants lip2p and lip2p2 are embryonic
CC lethal. {ECO:0000269|PubMed:23581459}.
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=AAD46029.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At1g47578 and At1g47580.; Evidence={ECO:0000305};
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DR EMBL; AC007519; AAD46029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32189.1; -; Genomic_DNA.
DR PIR; D96516; D96516.
DR RefSeq; NP_001185164.1; NM_001198235.2.
DR AlphaFoldDB; P0C7R2; -.
DR SMR; P0C7R2; -.
DR STRING; 3702.AT1G47578.1; -.
DR PaxDb; P0C7R2; -.
DR PRIDE; P0C7R2; -.
DR ProteomicsDB; 238660; -.
DR EnsemblPlants; AT1G47578.1; AT1G47578.1; AT1G47578.
DR GeneID; 10723096; -.
DR Gramene; AT1G47578.1; AT1G47578.1; AT1G47578.
DR KEGG; ath:AT1G47578; -.
DR Araport; AT1G47578; -.
DR TAIR; locus:6530298157; AT1G47578.
DR eggNOG; KOG0325; Eukaryota.
DR HOGENOM; CLU_035168_1_0_1; -.
DR InParanoid; P0C7R2; -.
DR OMA; VPCGIKS; -.
DR OrthoDB; 1491838at2759; -.
DR BioCyc; ARA:AT1G47578-MON; -.
DR BRENDA; 2.3.1.181; 399.
DR UniPathway; UPA00538; UER00592.
DR PRO; PR:P0C7R2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0C7R2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; 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 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; Chloroplast; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..280
FT /note="Octanoyltransferase LIP2p2, chloroplastic"
FT /id="PRO_0000342740"
FT DOMAIN 81..270
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT ACT_SITE 222
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P60720"
FT BINDING 123..130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 191..193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 188
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 280 AA; 32085 MW; 06CC5B07C66A2A8C CRC64;
MVFSVATSSV TNPKLHHHHH LSDFNRNRVS TSLKIMNSKN HTNPRKCECF DLYDQLIPYK
KAWSWQKSIL NEKKALIDKN QECSDSLIIL QHPSVYTMGT GSSENYLNFD IKNAPFDVYR
TERGGEVTYH GPGQLVMYPI INLRNHKMDL HWYLRKLEEV VIRVLSSAFA INASRLDGFT
GVWVGNKKMA AIGIRVSKWM TYHGLALNVT TDLTPFNSIV PCGIRNRGVG SVKGLIEDGE
HYNKLEDLQL LDIAHESLLK EFSEVFQLQM EKQTVFKLEC
