Q8W471 (AAE15_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Long-chain-fatty-acid--[acyl-carrier-protein] ligase AEE15, chloroplastic
EC=6.2.1.20

Alternative name(s):
Acyl-[acyl-carrier-protein] synthetase
Acyl-activating enzyme 15

Gene names

Name:	AAE15
Ordered Locus Names:	At4g14070
ORF Names:	dl3075c, FCAALL.81

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in the activation of fatty acids to acyl-carrier-protein prior to fatty acid elongation in plastids. Acts on medium- to long-chain fatty acids. Ref.1
Catalytic activity	ATP + an acid + [acyl-carrier-protein] = AMP + diphosphate + acyl-[acyl-carrier-protein]. Ref.1
Subcellular location	Plastid › chloroplast Probable.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Sequence caution	The sequence BAD94085.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB10186.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78449.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid elongation Inferred from direct assay Ref.1. Source: TAIR
Cellular_component	chloroplast envelope Inferred from direct assay PubMed 12766230PubMed 12938931PubMed 20061580. Source: TAIR
Molecular_function	long-chain fatty acid [acyl-carrier-protein] ligase activity Inferred from mutant phenotype Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 65	65	Chloroplast Potential
	Chain	66 – 727	662	Long-chain-fatty-acid--[acyl-carrier-protein] ligase AEE15, chloroplastic		PRO_0000415725
Experimental info
	Sequence conflict	318	1	Q → L in AAM28628. Ref.6
	Sequence conflict	595	1	G → A in AAM28628. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q8W471 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 059BBC287AB9F1C2	FASTA	727	81,466
	10 20 30 40 50 60 MQIRLKPDYS FFIASSSTMA STSSLGPSTL LSYGSPSRQF PDFGFRLISG HESVRIPSFR 70 80 90 100 110 120 RFRVHCESKE KEVKPSSPFL ESSSFSGDAA LRSSEWKAVP DIWRSSAEKY GDRVALVDPY 130 140 150 160 170 180 HDPPLKLTYK QLEQEILDFA EGLRVLGVKA DEKIALFADN SCRWLVSDQG IMATGAVNVV 190 200 210 220 230 240 RGSRSSVEEL LQIYRHSESV AIVVDNPEFF NRIAESFTSK ASLRFLILLW GEKSSLVTQG 250 260 270 280 290 300 MQIPVYSYAE IINQGQESRA KLSASNDTRS YRNQFIDSDD TAAIMYTSGT TGNPKGVMLT 310 320 330 340 350 360 HRNLLHQIKH LSKYVPAQAG DKFLSMLPSW HAYERASEYF IFTCGVEQMY TSIRYLKDDL 370 380 390 400 410 420 KRYQPNYIVS VPLVYETLYS GIQKQISASS AGRKFLALTL IKVSMAYMEM KRIYEGMCLT 430 440 450 460 470 480 KEQKPPMYIV AFVDWLWARV IAALLWPLHM LAKKLIYKKI HSSIGISKAG ISGGGSLPIH 490 500 510 520 530 540 VDKFFEAIGV ILQNGYGLTE TSPVVCARTL SCNVLGSAGH PMHGTEFKIV DPETNNVLPP 550 560 570 580 590 600 GSKGIIKVRG PQVMKGYYKN PSTTKQVLNE SGWFNTGDTG WIAPHHSKGR SRHCGGVIVL 610 620 630 640 650 660 EGRAKDTIVL STGENVEPLE IEEAAMRSRV IEQIVVIGQD RRRLGAIIIP NKEEAQRVDP 670 680 690 700 710 720 ETSKETLKSL VYQELRKWTS ECSFQVGPVL IVDDPFTIDN GLMTPTMKIR RDMVVAKYKE EIDQLYS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a plastid acyl-acyl carrier protein synthetase in Arabidopsis and its role in the activation and elongation of exogenous fatty acids." Koo A.J., Fulda M., Browse J., Ohlrogge J.B. Plant J. 44:620-632(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
[2]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that participate in fatty acid and glycerolipid metabolism." Shockey J.M., Fulda M.S., Browse J.A. Plant Physiol. 129:1710-1722(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-727.
[7]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 321-727. Strain: cv. Columbia.
[8]	"Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases." Shockey J.M., Fulda M.S., Browse J. Plant Physiol. 132:1065-1076(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF093797 mRNA. Translation: ABK88270.1. Z97335 Genomic DNA. Translation: CAB10186.1. Sequence problems. AL161538 Genomic DNA. Translation: CAB78449.1. Sequence problems. CP002687 Genomic DNA. Translation: AEE83367.1. AY062804 mRNA. Translation: AAL32882.1. BT010332 mRNA. Translation: AAQ56775.1. AF503770 mRNA. Translation: AAM28628.1. AK221841 mRNA. Translation: BAD94085.1. Different initiation.
IPI	IPI00543570.
PIR	H71401.
RefSeq	NP_193143.2. NM_117482.3.
UniGene	At.27227.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortal	Q8W471.
SMR	Q8W471. Positions 105-675.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G14070.1-P.
Proteomic databases
PRIDE	Q8W471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G14070.1; AT4G14070.1; AT4G14070.
GeneID	827043.
KEGG	ath:AT4G14070.
Organism-specific databases
GeneFarm	2213. 207.
TAIR	At4g14070.
Phylogenomic databases
eggNOG	COG1022.
HOGENOM	HOG000230013.
InParanoid	Q8W471.
KO	K01897.
OMA	RASEYFI.
PhylomeDB	Q8W471.
ProtClustDB	CLSN2690294.
Gene expression databases
ArrayExpress	Q8W471.
Genevestigator	Q8W471.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAE15_ARATH

Accession

Primary (citable) accession number: Q8W471
Secondary accession number(s): O23268, Q56X36, Q8LRT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program