LIP2P_ARATH
ID LIP2P_ARATH Reviewed; 278 AA.
AC Q948J9; O65544; O65545;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Octanoyltransferase LIP2p, chloroplastic {ECO:0000305};
DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:11602263};
DE AltName: Full=Lipoate-protein ligase 2p {ECO:0000305};
DE AltName: Full=Lipoyl-[acyl-carrier-protein]-protein-N-lipoyltransferase 2p {ECO:0000305};
DE AltName: Full=Plastidial lipoyltransferase 2 {ECO:0000303|PubMed:11602263};
DE Flags: Precursor;
GN Name=LIP2P {ECO:0000303|PubMed:11602263};
GN OrderedLocusNames=At4g31050 {ECO:0000312|Araport:AT4G31050};
GN ORFNames=F6I18.30 {ECO:0000312|EMBL:CAA18187.1},
GN F6I18.40 {ECO:0000312|EMBL:CAA18188.1};
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, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11602263; DOI=10.1016/s0014-5793(01)02932-5;
RA Wada M., Yasuno R., Wada H.;
RT "Identification of an Arabidopsis cDNA encoding a lipoyltransferase located
RT in plastids.";
RL FEBS Lett. 506:286-290(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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:11602263). Together with LIP1P is essential for de
CC novo plastidial protein lipoylation during seed development. Acts
CC redundantly with LIP2P2 (PubMed:23581459). {ECO:0000255|HAMAP-
CC Rule:MF_00013, ECO:0000269|PubMed:11602263,
CC 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:11602263};
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 -!- INTERACTION:
CC Q948J9; Q17TI5: BRX; NbExp=3; IntAct=EBI-25519006, EBI-4426649;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11602263, ECO:0000269|PubMed:23581459}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers
CC (PubMed:11602263, PubMed:23581459). Expressed in cauline leaves, stems
CC and siliques (PubMed:23581459). {ECO:0000269|PubMed:11602263,
CC 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=CAA18187.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g31060 has been split into 2 genes: At4g31060 and At4g31050.; Evidence={ECO:0000305};
CC Sequence=CAA18188.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79824.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g31060 has been split into 2 genes: At4g31060 and At4g31050.; Evidence={ECO:0000305};
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DR EMBL; AB072390; BAB69449.1; -; mRNA.
DR EMBL; AL022198; CAA18187.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL022198; CAA18188.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161578; CAB79823.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161578; CAB79824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85851.1; -; Genomic_DNA.
DR EMBL; AK221489; BAD94675.1; -; mRNA.
DR EMBL; BT024910; ABD91501.1; -; mRNA.
DR PIR; F85363; F85363.
DR PIR; G85363; G85363.
DR RefSeq; NP_567866.1; NM_119255.2.
DR AlphaFoldDB; Q948J9; -.
DR SMR; Q948J9; -.
DR BioGRID; 14519; 1.
DR IntAct; Q948J9; 1.
DR STRING; 3702.AT4G31050.1; -.
DR PaxDb; Q948J9; -.
DR PRIDE; Q948J9; -.
DR ProteomicsDB; 238438; -.
DR EnsemblPlants; AT4G31050.1; AT4G31050.1; AT4G31050.
DR GeneID; 829232; -.
DR Gramene; AT4G31050.1; AT4G31050.1; AT4G31050.
DR KEGG; ath:AT4G31050; -.
DR Araport; AT4G31050; -.
DR TAIR; locus:2126609; AT4G31050.
DR eggNOG; KOG0325; Eukaryota.
DR HOGENOM; CLU_035168_1_0_1; -.
DR InParanoid; Q948J9; -.
DR OMA; QWITYHG; -.
DR OrthoDB; 1491838at2759; -.
DR PhylomeDB; Q948J9; -.
DR BioCyc; ARA:AT4G31050-MON; -.
DR BRENDA; 2.3.1.181; 399.
DR UniPathway; UPA00538; UER00592.
DR PRO; PR:Q948J9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q948J9; baseline and differential.
DR Genevisible; Q948J9; AT.
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..19
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 20..278
FT /note="Octanoyltransferase LIP2p, chloroplastic"
FT /id="PRO_0000297760"
FT DOMAIN 79..267
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT ACT_SITE 220
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P60720"
FT BINDING 121..128
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 189..191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 186
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 278 AA; 31859 MW; 1ED66821BA7F8783 CRC64;
MELLNGVETL VSGIHHHHRT NAKRNRLVRS VKILNSGNHE IPRKCLCFDL YDKLVPYKKA
WSWQKSIVEE KKTLIDRNQD CADTVILLQH SPVYTMGTAS TEDYLNFDIK DAPFNVYRTE
RGGEVTYHGP GQLVMYPIIN LRNHEMDLHW YLRMLEEIVI RVLSSTFSIK ASRLDGLTGV
WVGNQKVAAI GIRVSKWITY HGLALNVTTD LTPFNWIVPC GIRDRKVGNI KGLLEDGEHG
MVDDLRLIDI VHESLLKEFS EAFQLQIEKQ TVSDPNIL
