Information on EC 5.2.1.B4 - 2-methyl-cis-aconitate isomerase

for references in articles please use BRENDA:EC5.2.1.B4

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preliminary BRENDA-supplied EC number

EC Tree 5 Isomerases 5.2 cis-trans-Isomerases 5.2.1 cis-trans Isomerases (only sub-subclass identified to date) 5.2.1.B4 2-methyl-cis-aconitate isomerase

The expected taxonomic range for this enzyme is: Shewanella oneidensis

Reaction Schemes

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(1Z,3R)-but-1-ene-1,2,3-tricarboxylate

(2Z)-but-2-ene-1,2,3-tricarboxylate

Synonyms
prpf protein, more

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

2-methyl-aconitate isomerase

Shewanella oneidensis

Q8EJW4

749113

PrpF protein

Shewanella oneidensis

Q8EJW4

749113

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

(1Z,3R)-but-1-ene-1,2,3-tricarboxylate = (2Z)-but-2-ene-1,2,3-tricarboxylate

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

Reversibility
r=reversible
ir=irreversible
?=not specified

(R)-4-methyl-cis-aconitate

2-methyl-cis-aconitate

2 entries

(R)-4-methyl-cis-aconitate

2-methyl-cis-aconitate

Shewanella oneidensis

Q8EJW4

749113

Substrates: the enzyme is involved in catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle. The 2-methylcitric acid cycle is a common route of propionate catabolism in microorganisms
Products: -

(R)-4-methyl-cis-aconitate

2-methyl-cis-aconitate

Shewanella oneidensis

Q8EJW4

749113

Substrates: -
Products: -

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

(R)-4-methyl-cis-aconitate

2-methyl-cis-aconitate

Shewanella oneidensis

Q8EJW4

749113

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only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Shewanella oneidensis

749113

Q8EJW4

SwissProt

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

Shewanella oneidensis

Q8EJW4

the enzyme is involved in catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle. The 2-methylcitric acid cycle is a common route of propionate catabolism in microorganisms

749113

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

Q8EJW4 pBLAST

PRPF_SHEON

Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)

397

41660

Swiss-Prot

Show Sequence

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging drop vapor diffusion method, high-resolution three-dimensional crystal structures of mutant enzyme K73E in complex with trans-aconitate or malonate provides insights into the mechanism of catalysis of the wild-type protein

Shewanella oneidensis

Q8EJW4

749113

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

C107A

Shewanella oneidensis

Q8EJW4

protein containing the C107A substitution is not overproduced and could not be purified

749113

C107S

Shewanella oneidensis

Q8EJW4

inactive mutant enzyme

749113

K73A

Shewanella oneidensis

Q8EJW4

protein containing the K73A substitution is not overproduced and could not be purified

749113

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

749113

Rocco, C.J.; Wetterhorn, K.M.; Garvey, G.S.; Rayment, I.; Escalante-Semerena, J.C.

The PrpF protein of Shewanella oneidensis MR-1 catalyzes the isomerization of 2-methyl-cis-aconitate during the catabolism of propionate via the AcnD-dependent 2-methylcitric acid cycle

PLoS ONE

e0188130

2017

Shewanella oneidensis (Q8EJW4), Shewanella oneidensis

29145506

brenda

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EXTERNAL LINKS (specific for EC-Number 5.2.1.B4)

ExplorEnz (official portal for IUBMB Enzyme Nomenclature)

Expasy Enzyme Nomenclature Database

KEGG

SABIO-RK

NCBI: PubMed, Protein, Nucleotide, Structure, Gene, OMIM

Enzyme Nomenclature (alternative site)

UniProt

PDB

PROSITE Database of protein families and domains

InterPro (database of protein families, domains and functional sites)

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