2-oxoglutarate-dependent ethylene/succinate-forming enzyme - Pseudomonas syringae pv. phaseolicola

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P32021 (EFE_PSESH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 67. History...

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

Documents (2) |

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:
2-oxoglutarate-dependent ethylene/succinate-forming enzyme
Short name=EFE
Short name=Ethylene-forming enzyme
EC=1.13.12.19
EC=1.14.11.34

Alternative name(s):
2-oxoglutarate dioxygenase (ethylene-forming)
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)

Gene names

Name:

efe

Encoded on

Plasmid pPSP1

Organism

Pseudomonas syringae pv. phaseolicola

Taxonomic identifier

319 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Simultaneously catalyzes two reactions, namely formation of ethylene and of succinate from 2-oxoglutarate, with a molar ratio of 2:1. Ref.3
Catalytic activity	2-oxoglutarate + O₂ = ethylene + 3 CO₂ + H₂O. 2-oxoglutarate + L-arginine + O₂ = succinate + CO₂ + guanidine + (S)-1-pyrroline-5-carboxylate + H₂O.
Cofactor	Fe²⁺.
Enzyme regulation	Activated by catalase. Inhibited by chelating reagents such as EDTA and Tiron (4,5-dihydroxy-1,3-benzene disulphonic acid), and by DTNB (5,5'-dithio-bis-2-nitrobenzoate) and hydrogen peroxide.
Pathway	Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate.
Subunit structure	Monomer.
Miscellaneous	A dual-circuit mechanism has been proposed in Ref.3 for the complete reaction, in which the binding of L-arginine and 2-oxoglutarate in a Schiff-base structure generates a common intermediate for the two reactions.
Sequence similarities	Belongs to the iron/ascorbate-dependent oxidoreductase family. Contains 1 Fe2OG dioxygenase domain.
Biophysicochemical properties	Kinetic parameters: K_M=59 µM for Fe²⁺ K_M=19 µM for 2-oxoglutarate K_M=18 µM for L-arginine pH dependence: Optimum pH is 7.0-7.5. Temperature dependence: Optimum temperature is 20-25 degrees Celsius.

Ontologies

Keywords
Biological process	Ethylene biosynthesis
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological_process	ethylene biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	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 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 350

350

2-oxoglutarate-dependent ethylene/succinate-forming enzyme

PRO_0000067277

Regions

Domain

166 – 286

121

Fe2OG dioxygenase

Sites

Metal binding

189

Iron Potential

Metal binding

268

Iron Potential

Experimental info

Sequence conflict

W → K AA sequence Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P32021 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 5FD86F07EFCD392B
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FASTA

350

39,445

        10         20         30         40         50         60 
MTNLQTFELP TEVTGCAADI SLGRALIQAW QKDGIFQIKT DSEQDRKTQE AMAASKQFCK 

        70         80         90        100        110        120 
EPLTFKSSCV SDLTYSGYVA SGEEVTAGKP DFPEIFTVCK DLSVGDQRVK AGWPCHGPVP 

       130        140        150        160        170        180 
WPNNTYQKSM KTFMEELGLA GERLLKLTAL GFELPINTFT DLTRDGWHHM RVLRFPPQTS 

       190        200        210        220        230        240 
TLSRGIGAHT DYGLLVIAAQ DDVGGLYIRP PVEGEKRNRN WLPGESSAGM FEHDEPWTFV 

       250        260        270        280        290        300 
TPTPGVWTVF PGDILQFMTG GQLLSTPHKV KLNTRERFAC AYFHEPNFEA SAYPLFEPSA 

       310        320        330        340        350 
NERIHYGEHF TNMFMRCYPD RITTQRINKE NRLAHLEDLK KYSDTRATGS

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References

[1]	"Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2." Fukuda H., Ogawa T., Ishihara K., Fujii T., Nagahama K., Omata T., Inoue Y., Tanase S., Morino Y. Biochem. Biophys. Res. Commun. 188:826-832(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PK2.
[2]	"Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2." Nagahama K., Ogawa T., Fujii T., Tazaki M., Tanase S., Morino Y., Fukuda H. J. Gen. Microbiol. 137:2281-2286(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-30, CHARACTERIZATION. Strain: PK2.
[3]	"Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae." Fukuda H., Ogawa T., Tazaki M., Nagahama K., Fujii T., Tanase S., Morino Y. Biochem. Biophys. Res. Commun. 188:483-489(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MECHANISM. Strain: PK2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13182 Genomic DNA. Translation: BAA02477.1.
PIR	JQ1656.
3D structure databases
ProteinModelPortal	P32021.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16773.
SABIO-RK	P32021.
UniPathway	UPA00385.
Family and domain databases
Gene3D	2.60.120.330. 1 hit.
InterPro	IPR026992. DIOX_N. IPR027443. IPNS-like. 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

EFE_PSESH

Accession

Primary (citable) accession number: P32021

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

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

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