Reviewed, UniProtKB/Swiss-Prot P33207 (FABG_ARATH)

Names and origin

Protein names

Recommended name:
    3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
    EC=1.1.1.100
Alternative name(s):
    3-ketoacyl-acyl carrier protein reductase

Gene names

Ordered Locus Names:	At1g24360
ORF Names:	F21J9.2, F3I6.30

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subunit structure	Homotetramer Probable.
Subcellular location	Plastid › chloroplast. Plastid. Note: And non-photosynthetic plastids.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Sequence caution	The sequence AAC00590.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAF97951.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	3-oxoacyl-[acyl-carrier-protein] reductase activity Inferred from electronic annotation. Source: EC NAD or NADH binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 59	59	Chloroplast By similarity
	Chain	60 – 319	260	3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic		PRO_0000031976
Regions
	Nucleotide binding	81 – 105	25	NADP By similarity
Sites
	Active site	226	1	Proton acceptor By similarity
	Binding site	213	1	Substrate By similarity
Experimental info
	Sequence conflict	17	1	A → G in CAA45794. Ref.1
	Sequence conflict	227 – 229	3	AAA → TAT in CAA45794. Ref.1
	Sequence conflict	238 – 240	3	KTA → ETP in CAA45794. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P33207-1 [UniParc]. Last modified January 10, 2003. Version 2. Checksum: 755ADDD16F3F69DE	FASTA	319	33,548
	10 20 30 40 50 60 MAAAVAAPRL ISLKAVAKLG FREISQIRQL APLHSAIPHF GMLRCRSRQP FSTSVVKAQA 70 80 90 100 110 120 TATEQSPGEV VQKVESPVVV ITGASRGIGK AIALALGKAG CKVLVNYARS AKEAEEVAKQ 130 140 150 160 170 180 IEEYGGQAIT FGGDVSKATD VDAMMKTALD KWGTIDVVVN NAGITRDTLL IRMKQSQWDE 190 200 210 220 230 240 VIALNLTGVF LCTQAAVKIM MKKKRGRIIN ISSVVGLIGN IGQANYAAAK GGVISFSKTA 250 260 270 280 290 300 AREGASRNIN VNVVCPGFIA SDMTAELGED MEKKILGTIP LGRYGKAEEV AGLVEFLALS 310 PAASYITGQA FTIDGGIAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of higher-plant 3-oxoacyl-(acyl carrier protein) reductase. Sequence identities with the nodG-gene product of the nitrogen-fixing soil bacterium Rhizobium meliloti." Slabas A.R., Chase D., Nishida I., Murata N., Sidebottom C.M., Safford R., Sheldon P.S., Kekwick R.G.O., Hardie D.G., Mackintosh R.W. Biochem. J. 283:321-326(1992) [PubMed: 1575676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf.
[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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X64464 mRNA. Translation: CAA45794.1. AC000103 Genomic DNA. Translation: AAF97951.1. Sequence problems. AC002396 Genomic DNA. Translation: AAC00590.1. Sequence problems. AF324985 mRNA. Translation: AAG40337.1. AY059816 mRNA. Translation: AAL24298.1. AY081491 mRNA. Translation: AAM10053.1.
IPI	IPI00543619.
PIR	A86378. S22416. T00667.
RefSeq	NP_564216.1.
UniGene	At.4
3D structure databases
HSSP	HSSP built from PDB template 1EDO based on UniProtKB Q93X62.
SMR	P33207. Positions 76-319.
ModBase	Search...
Protein-protein interaction databases
STRING	P33207.
Proteomic databases
PRIDE	P33207.
Genome annotation databases
GeneID	839053.
GenomeReviews	Gene locus AT1G24360 in contig CT485782_GR.
KEGG	ath:AT1G24360.
NMPDR	fig|3702.1.peg.2830.
Organism-specific databases
TAIR	At1g24360.
Phylogenomic databases
OMA	LLRMKES.
Enzyme and pathway databases
BRENDA	1.1.1.100. 302.
Gene expression databases
ArrayExpress	P33207.
Genevestigator	P33207.
GermOnline	AT1G24360. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011284. 3oxo_ACP_reduc. IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR19410. ADH_short_C2. 1 hit.
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
TIGRFAMs	TIGR01830. 3oxo_ACP_reduc. 1 hit.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FABG_ARATH

Accession

Primary (citable) accession number: P33207
Secondary accession number(s): O04463, Q9FPJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 10, 2003
Last modified:	November 3, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)