1-aminocyclopropane-1-carboxylate oxidase 1 - Arabidopsis thaliana (Mouse-ear cress)

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Q9ZUN4 (ACCO1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
1-aminocyclopropane-1-carboxylate oxidase 1
Short name=ACC oxidase 1
Short name=AtACO1
EC=1.14.17.4

Gene names

Name:	ACO1
Ordered Locus Names:	At2g19590
ORF Names:	F3P11.19

Organism

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

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

General annotation (Comments)

Function	Enzyme involved in the ethylene biosynthesis. May promote stem elongation by maximizing the extensibility cells, possibly by activating ethylene biosynthesis, in response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0). Ref.8
Catalytic activity	1-aminocyclopropane-1-carboxylate + ascorbate + O₂ = ethylene + cyanide + dehydroascorbate + CO₂ + 2 H₂O.
Cofactor	Binds 1 Fe²⁺ ion per subunit By similarity.
Pathway	Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
Induction	Upon potassium K⁺ and iron deprivation. Induced in leaf blades in low light intensities. Seems repressed by ethylene. Accumulates in response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0). Induced in roots by nitric oxide (NO). Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
Biological process	Ethylene biosynthesis Plant defense
Domain	Coiled coil
Ligand	Iron Metal-binding Vitamin C
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to fatty acid Inferred from expression pattern Ref.8. Source: UniProtKB cellular response to iron ion Inferred from expression pattern Ref.9. Source: TAIR cellular response to nitric oxide Inferred from expression pattern Ref.10. Source: UniProtKB cellular response to potassium ion starvation Inferred from expression pattern Ref.6. Source: UniProtKB defense response Inferred from electronic annotation. Source: UniProtKB-KW ethylene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	1-aminocyclopropane-1-carboxylate oxidase activity Inferred from electronic annotation. Source: EC L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 310

310

1-aminocyclopropane-1-carboxylate oxidase 1

PRO_0000408297

Regions

Domain

158 – 259

102

Fe2OG dioxygenase

Coiled coil

113 – 133

Potential

Sites

Metal binding

182

Iron By similarity

Metal binding

184

Iron By similarity

Metal binding

240

Iron By similarity

Binding site

250

2-oxoglutarate Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZUN4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 8CA84DFBEC4E1647
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FASTA

310

35,202

        10         20         30         40         50         60 
MVLIKEREME IPVIDFAELD GEKRSKTMSL LDHACDKWGF FMVDNHGIDK ELMEKVKKMI 

        70         80         90        100        110        120 
NSHYEEHLKE KFYQSEMVKA LSEGKTSDAD WESSFFISHK PTSNICQIPN ISEELSKTMD 

       130        140        150        160        170        180 
EYVCQLHKFA ERLSKLMCEN LGLDQEDIMN AFSGPKGPAF GTKVAKYPEC PRPELMRGLR 

       190        200        210        220        230        240 
EHTDAGGIIL LLQDDQVPGL EFFKDGKWVP IPPSKNNTIF VNTGDQLEIL SNGRYKSVVH 

       250        260        270        280        290        300 
RVMTVKHGSR LSIATFYNPA GDAIISPAPK LLYPSGYRFQ DYLKLYSTTK FGDKGPRLET 

       310 
MKKMGNADSA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Ethylene and auxin control the Arabidopsis response to decreased light intensity." Vandenbussche F., Vriezen W.H., Smalle J., Laarhoven L.J.J., Harren F.J.M., Van Der Straeten D. Plant Physiol. 133:517-527(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY LOW LIGHT.
[5]	"Transcriptional profiling by cDNA-AFLP and microarray analysis reveals novel insights into the early response to ethylene in Arabidopsis." De Paepe A., Vuylsteke M., Van Hummelen P., Zabeau M., Van Der Straeten D. Plant J. 39:537-559(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY ETHYLENE. Strain: cv. Columbia.
[6]	"Hydrogen peroxide mediates plant root cell response to nutrient deprivation." Shin R., Schachtman D.P. Proc. Natl. Acad. Sci. U.S.A. 101:8827-8832(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY POTASSIUM DEPRIVATION.
[7]	"The potassium transporter AtHAK5 functions in K(+) deprivation-induced high-affinity K(+) uptake and AKT1 K(+) channel contribution to K(+) uptake kinetics in Arabidopsis roots." Gierth M., Maeser P., Schroeder J.I. Plant Physiol. 137:1105-1114(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY POTASSIUM DEPRIVATION.
[8]	"Saturated very-long-chain fatty acids promote cotton fiber and Arabidopsis cell elongation by activating ethylene biosynthesis." Qin Y.-M., Hu C.-Y., Pang Y., Kastaniotis A.J., Hiltunen J.K., Zhu Y.-X. Plant Cell 19:3692-3704(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION BY VERY-LONG-CHAIN FATTY ACIDS. Strain: cv. Columbia.
[9]	"Ethylene and nitric oxide involvement in the up-regulation of key genes related to iron acquisition and homeostasis in Arabidopsis." Garcia M.J., Lucena C., Romera F.J., Alcantara E., Perez-Vicente R. J. Exp. Bot. 61:3885-3899(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY IRON DEFICIENCY.
[10]	"A new model involving ethylene, nitric oxide and Fe to explain the regulation of Fe-acquisition genes in Strategy I plants." Garcia M.J., Suarez V., Romera F.J., Alcantara E., Perez-Vicente R. Plant Physiol. Biochem. 49:537-544(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY NITRIC OXIDE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC005917 Genomic DNA. Translation: AAD10157.1. CP002685 Genomic DNA. Translation: AEC06898.1. AF370195 mRNA. Translation: AAK44010.1. AY062951 mRNA. Translation: AAL33783.1.
IPI	IPI00547822.
PIR	F84578.
RefSeq	NP_179549.1. NM_127517.4.
UniGene	At.24322. At.67077. At.67755.
3D structure databases
HSSP	HSSP built from PDB template 1GP5 based on UniProtKB Q96323.
ProteinModelPortal	Q9ZUN4.
SMR	Q9ZUN4. Positions 12-304.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT2G19590.1-P.
Proteomic databases
PaxDb	Q9ZUN4.
PRIDE	Q9ZUN4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G19590.1; AT2G19590.1; AT2G19590.
GeneID	816478.
KEGG	ath:AT2G19590.
Organism-specific databases
TAIR	At2g19590.
Phylogenomic databases
eggNOG	COG3491.
HOGENOM	HOG000276735.
InParanoid	Q9ZUN4.
KO	K05933.
OMA	TIFVNTG.
PhylomeDB	Q9ZUN4.
ProtClustDB	PLN02403.
Enzyme and pathway databases
UniPathway	UPA00384; UER00563.
Gene expression databases
Genevestigator	Q9ZUN4.
Family and domain databases
InterPro	IPR026992. DIOX_N. IPR005123. Oxoglu/Fe-dep_dioxygenase. [Graphical view]
Pfam	PF03171. 2OG-FeII_Oxy. 1 hit. PF14226. DIOX_N. 1 hit. [Graphical view]
PROSITE	PS51471. FE2OG_OXY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCO1_ARATH

Accession

Primary (citable) accession number: Q9ZUN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 3, 2011
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents