Q08506 (ACCO1_PETHY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Ethylene-forming enzyme
Short name=EFE

Gene names

Name:

ACO1

Organism

Petunia hybrida (Petunia)

Taxonomic identifier

4102 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Petunioideae › Petunia

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O.
Cofactor	Iron. Ref.2
Pathway	Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.

Ontologies

Keywords
Biological process	Ethylene biosynthesis
Ligand	Iron Metal-binding Vitamin C
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	ethylene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – 319

319

1-aminocyclopropane-1-carboxylate oxidase 1

PRO_0000067271

Regions

Domain

153 – 253

101

Fe2OG dioxygenase

Sites

Metal binding

177

1

Iron

Metal binding

179

1

Iron

Metal binding

234

1

Iron

Secondary structure

1

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319

Helix Strand Turn

Details...

Beta strand

6 – 8

3

Helix

9 – 13

5

Helix

17 – 30

14

Beta strand

32 – 38

7

Helix

43 – 74

32

Helix

81 – 83

3

Beta strand

88 – 96

9

Helix

99 – 102

4

Helix

108 – 136

29

Helix

142 – 148

7

Turn

149 – 151

3

Beta strand

154 – 161

8

Helix

168 – 171

4

Beta strand

180 – 191

12

Beta strand

195 – 199

5

Beta strand

202 – 205

4

Beta strand

213 – 217

5

Helix

219 – 224

6

Turn

225 – 227

3

Beta strand

234 – 236

3

Beta strand

240 – 242

3

Beta strand

245 – 252

8

Helix

263 – 265

3

Helix

282 – 287

6

Turn

288 – 293

6

Helix

297 – 306

10

Sequences

	Sequence		Length	Mass (Da)
	Q08506 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: B17768B2B5E0CE82	FASTA	319	36,187
	10 20 30 40 50 60 MENFPIISLD KVNGVERAAT MEMIKDACEN WGFFELVNHG IPREVMDTVE KMTKGHYKKC 70 80 90 100 110 120 MEQRFKELVA SKALEGVQAE VTDMDWESTF FLKHLPISNI SEVPDLDEEY REVMRDFAKR 130 140 150 160 170 180 LEKLAEELLD LLCENLGLEK GYLKNAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA 190 200 210 220 230 240 GGIILLFQDD KVSGLQLLKD GQWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVMHRVIAQK 250 260 270 280 290 300 DGARMSLASF YNPGSDAVIY PAPALVEKEA EENKQVYPKF VFDDYMKLYA GLKFQAKEPR 310 FEAMKAMETD VKMDPIATV

References

[1]	"Organization and structure of the 1-aminocyclopropane-1-carboxylate oxidase gene family from Petunia hybrida." Tang X., Wang H., Brandt A.S., Woodson W.R. Plant Mol. Biol. 23:1151-1164(1993) [PubMed: 8292780] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase -- the ethylene-forming enzyme." Zhang Z., Ren J.-S., Clifton I.J., Schofield C.J. Chem. Biol. 11:1383-1394(2004) [PubMed: 15489165] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), COFACTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L21976 Unassigned DNA. Translation: AAC37381.1.

PIR

S42560.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W9Y	X-ray	2.10	A	1-319	[»]
1WA6	X-ray	2.55	X	1-319	[»]

ProteinModelPortal

Q08506.

SMR

Q08506. Positions 2-307.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR005123. Oxoglutarate/Fe-dep_oxygenase.
[Graphical view]

Pfam

PF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]

PROSITE

PS51471. FE2OG_OXY. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACCO1_PETHY

Accession

Primary (citable) accession number: Q08506

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	October 19, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program