Q8L3X9 (KASM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
EC=2.3.1.41

Alternative name(s):
Beta-ketoacyl-ACP synthase
mtKAS

Gene names

Name:	KAS
Ordered Locus Names:	At2g04540
ORF Names:	T1O3.5

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	461 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	Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16.
Catalytic activity	Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
Enzyme regulation	Inhibited by cerulenin.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Mitochondrion Ref.1.
Tissue specificity	Expressed at the same level in leaves, roots and flowers. Ref.1
Sequence similarities	Belongs to the beta-ketoacyl-ACP synthases family.
Sequence caution	The sequence AAD25826.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 28

28

Mitochondrion Potential

Chain

29 – 461

433

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

PRO_0000000588

Regions

Compositional bias

139 – 144

6

Poly-Glu

Sites

Active site

209

1

By similarity

Secondary structure

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461

Helix Strand Turn

Details...

Beta strand

33 – 42

10

Beta strand

45 – 47

3

Helix

48 – 56

9

Beta strand

62 – 64

3

Helix

68 – 70

3

Helix

77 – 85

9

Beta strand

91 – 93

3

Beta strand

97 – 100

4

Helix

106 – 109

4

Helix

117 – 132

16

Helix

140 – 144

5

Beta strand

146 – 154

9

Helix

157 – 168

12

Helix

172 – 174

3

Helix

179 – 183

5

Helix

187 – 196

10

Helix

208 – 210

3

Helix

211 – 225

15

Beta strand

229 – 237

9

Helix

242 – 250

9

Turn

257 – 260

4

Helix

262 – 264

3

Beta strand

281 – 289

9

Helix

290 – 295

6

Beta strand

302 – 311

10

Helix

324 – 337

14

Helix

341 – 343

3

Beta strand

346 – 348

3

Helix

355 – 369

15

Helix

371 – 374

4

Beta strand

378 – 381

4

Helix

384 – 387

4

Helix

391 – 393

3

Helix

394 – 408

15

Beta strand

418 – 420

3

Beta strand

426 – 428

3

Beta strand

440 – 448

9

Turn

449 – 451

3

Beta strand

452 – 459

8

Sequences

	Sequence		Length	Mass (Da)
	Q8L3X9 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: D9B02B19F5A5FB45	FASTA	461	49,379
	10 20 30 40 50 60 MATSNLRRHL SASRLRLNRF ISTSSSYHSH RRVVVTGLGM VTPLGRGVET TWRRLIDGEC 70 80 90 100 110 120 GIRGLTLDDL KMKSFDEETK LYTFDQLSSK VAAFVPYGSN PGEFDEALWL NSKAVANFIG 130 140 150 160 170 180 YAVCAADEAL RDAEWLPTEE EEKERTGVSI GGGIGSICDI VEAAQLICEK RLRRLSPFFI 190 200 210 220 230 240 PKILVNMASG HVSMKYGFQG PNHAAVTACA TGAHSIGDAT RMIQFGDADV MVAGGTESSI 250 260 270 280 290 300 DALSVAGFSR SRALSTKFNS SPQEASRPFD CDRDGFVIGE GSGVIVLEEY EHAKRRGAKI 310 320 330 340 350 360 YAELCGYGMS GDAHHITQPP EDGKGAVLAM TRALRQSGLC PNQIDYVNAH ATSTPIGDAV 370 380 390 400 410 420 EARAIKTVFS EHATSGTLAF SSTKGATGHL LGAAGAVEAI FSILAIHHGV APMTLNVKNP 430 440 450 460 DPIFDKRFMP LTTSKKMLVR TAMSNSFGFG GTNASLLFAS I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and molecular characterization of the beta-ketoacyl-[acyl carrier-protein] synthase component of the Arabidopsis mitochondrial fatty acid synthase." Yasuno R., von Wettstein-Knowles P., Wada H. J. Biol. Chem. 279:8242-8251(2004) [PubMed: 14660674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Structure of the mitochondrial beta-ketoacyl-[acyl carrier-protein] synthase from Arabidopsis and its role in fatty acid synthesis." Olsen J.G., Rasmussen A.V., von Wettstein-Knowles P., Henriksen A. FEBS Lett. 577:170-174(2004) [PubMed: 15527780] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-461.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB073746 mRNA. Translation: BAB91181.1.
AC006951 Genomic DNA. Translation: AAD25826.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC05844.1.
AY099587 mRNA. Translation: AAM20439.1.
AY128832 mRNA. Translation: AAM91232.1.

IPI

IPI00530183.

PIR

F84458.

RefSeq

NP_178533.2. NM_126485.3.

UniGene

At.41299.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W0I	X-ray	2.10	A/B	31-461	[»]
2IX4	X-ray	1.95	A/B	31-461	[»]

ProteinModelPortal

Q8L3X9.

SMR

Q8L3X9. Positions 31-461.

ModBase

Search...

Protein-protein interaction databases

STRING

Q8L3X9.

Proteomic databases

PRIDE

Q8L3X9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT2G04540.1; AT2G04540.1; AT2G04540.

GeneID

814996.

GenomeReviews

Gene locus AT2G04540 in contig CT485783_GR.

KEGG

ath:AT2G04540.

NMPDR

fig|3702.1.peg.8037.

Organism-specific databases

TAIR

At2g04540.

Phylogenomic databases

eggNOG

KOG1394.

GeneTree

EPGT00070000029170.

HOGENOM

HBG757733.

InParanoid

Q8L3X9.

OMA

ENKAIKH.

PhylomeDB

Q8L3X9.

ProtClustDB

PLN02836.

Enzyme and pathway databases

BioCyc

MetaCyc:AT2G04540-MONOMER.

BRENDA

2.3.1.41. 399.

Gene expression databases

Genevestigator

Q8L3X9.

GermOnline

AT2G04540. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR017568. 3-oxoacyl-ACP_synth-2.
IPR000794. Beta-ketoacyl_synthase.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.

KO

K09458.

PANTHER

PTHR11712. Ketoacyl_synth. 1 hit.

Pfam

PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000447. KAS_II. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

TIGRFAMs

TIGR03150. FabF. 1 hit.

PROSITE

PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KASM_ARATH

Accession

Primary (citable) accession number: Q8L3X9
Secondary accession number(s): Q9SJB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	October 1, 2002
Last modified:	November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program