Q9CAP8 (LACS9_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Long chain acyl-CoA synthetase 9, chloroplastic
EC=6.2.1.3

Gene names

Name:	LACS9
Ordered Locus Names:	At1g77590
ORF Names:	T5M16.18

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	691 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate. Ref.6
Catalytic activity	ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.1
Cofactor	Magnesium By similarity.
Pathway	Lipid metabolism; fatty acid metabolism.
Subcellular location	Plastid › chloroplast envelope Ref.6.
Tissue specificity	Highly expressed in developing seeds and young rosette leaves. Ref.6
Disruption phenotype	Reduced amount long-chain fatty acid (LCFA). Ref.6
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Chloroplast Plastid
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	chloroplast envelope Inferred from direct assay PubMed 12766230PubMed 12938931PubMed 20061580. Source: TAIR membrane Inferred from direct assay PubMed 17432890. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 691	691	Long chain acyl-CoA synthetase 9, chloroplastic		PRO_0000401418
Regions
	Nucleotide binding	250 – 261	12	ATP Potential
	Region	525 – 553	29	Fatty acid-binding Potential
Experimental info
	Sequence conflict	293	1	Y → F in AAO22689. Ref.4
	Sequence conflict	586 – 587	2	AD → SS in BAF01957. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9CAP8 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8B01B936CF91F564	FASTA	691	76,176
	10 20 30 40 50 60 MIPYAAGVIV PLALTFLVQK SKKEKKRGVV VDVGGEPGYA IRNHRFTEPV SSHWEHISTL 70 80 90 100 110 120 PELFEISCNA HSDRVFLGTR KLISREIETS EDGKTFEKLH LGDYEWLTFG KTLEAVCDFA 130 140 150 160 170 180 SGLVQIGHKT EERVAIFADT REEWFISLQG CFRRNVTVVT IYSSLGEEAL CHSLNETEVT 190 200 210 220 230 240 TVICGSKELK KLMDISQQLE TVKRVICMDD EFPSDVNSNW MATSFTDVQK LGRENPVDPN 250 260 270 280 290 300 FPLSADVAVI MYTSGSTGLP KGVMMTHGNV LATVSAVMTI VPDLGKRDIY MAYLPLAHIL 310 320 330 340 350 360 ELAAESVMAT IGSAIGYGSP LTLTDTSNKI KKGTKGDVTA LKPTIMTAVP AILDRVRDGV 370 380 390 400 410 420 RKKVDAKGGL SKKLFDFAYA RRLSAINGSW FGAWGLEKLL WDVLVFRKIR AVLGGQIRYL 430 440 450 460 470 480 LSGGAPLSGD TQRFINICVG APIGQGYGLT ETCAGGTFSE FEDTSVGRVG APLPCSFVKL 490 500 510 520 530 540 VDWAEGGYLT SDKPMPRGEI VIGGSNITLG YFKNEEKTKE VYKVDEKGMR WFYTGDIGRF 550 560 570 580 590 600 HPDGCLEIID RKKDIVKLQH GEYVSLGKVE AALSISPYVE NIMVHADSFY SYCVALVVAS 610 620 630 640 650 660 QHTVEGWASK QGIDFANFEE LCTKEQAVKE VYASLVKAAK QSRLEKFEIP AKIKLLASPW 670 680 690 TPESGLVTAA LKLKRDVIRR EFSEDLTKLY A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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], GENE FAMILY, ENZYME ACTIVITY.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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] OF 293-691. Strain: cv. Columbia.
[5]	"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 (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-691. Strain: cv. Columbia.
[6]	"Fatty acid export from the chloroplast. Molecular characterization of a major plastidial acyl-coenzyme A synthetase from Arabidopsis." Schnurr J.A., Shockey J.M., de Boer G.J., Browse J.A. Plant Physiol. 129:1700-1709(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.
[7]	"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 ORGANIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF503759 mRNA. Translation: AAM28876.1. AC010704 Genomic DNA. Translation: AAG51668.1. CP002684 Genomic DNA. Translation: AEE35996.1. BT002872 mRNA. Translation: AAO22689.1. AK230143 mRNA. Translation: BAF01957.1.
IPI	IPI00540420.
PIR	D96805.
RefSeq	NP_177882.1. NM_106407.6.
UniGene	At.28137.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ProteinModelPortal	Q9CAP8.
SMR	Q9CAP8. Positions 105-683.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT1G77590.1-P.
Proteomic databases
PaxDb	Q9CAP8.
PRIDE	Q9CAP8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G77590.1; AT1G77590.1; AT1G77590.
GeneID	844094.
KEGG	ath:AT1G77590.
Organism-specific databases
TAIR	At1g77590.
Phylogenomic databases
eggNOG	COG1022.
HOGENOM	HOG000159459.
InParanoid	Q9CAP8.
KO	K01897.
OMA	NQIKAKP.
PhylomeDB	Q9CAP8.
ProtClustDB	PLN02387.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G77590-MONOMER.
UniPathway	UPA00199.
Gene expression databases
Genevestigator	Q9CAP8.
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

LACS9_ARATH

Accession

Primary (citable) accession number: Q9CAP8
Secondary accession number(s): Q0WLQ0, Q84WQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 30, 2010
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program