P56839 (PEPM_MYTED) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Phosphoenolpyruvate phosphomutase Short name=PEP mutase Short name=PEP phosphomutase Short name=Phosphoenolpyruvate mutase EC=5.4.2.9
Organism	Mytilus edulis (Blue mussel)
Taxonomic identifier	6550 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Bivalvia › Pteriomorphia › Mytiloida › Mytiloidea › Mytilidae › Mytilinae › Mytilus

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
Catalytic activity	Phosphoenolpyruvate = 3-phosphonopyruvate.
Cofactor	Magnesium.
Pathway	Phosphorus metabolism; phosphonate biosynthesis.
Subunit structure	Homotetramer. Ref.1 Ref.2
Sequence similarities	Belongs to the isocitrate lyase/PEP mutase superfamily. PEP mutase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	organic phosphonate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 295

294

Phosphoenolpyruvate phosphomutase

PRO_0000068824

Sites

Active site

58

1

Nucleophile Potential

Metal binding

58

1

Magnesium

Experimental info

Mutagenesis

58

1

D → A or S: Abolishes enzyme activity. Ref.1 Ref.3

Mutagenesis

58

1

D → N: Strongly reduces enzyme activity. Ref.1 Ref.3

Mutagenesis

85

1

D → A: Strongly reduces enzyme activity and increases KM. Ref.1

Mutagenesis

87

1

D → A: Strongly reduces enzyme activity. Ref.1

Mutagenesis

114

1

E → A: Strongly reduces enzyme activity. Ref.1

Mutagenesis

122

1

N → A or D: Strongly reduces enzyme activity. Ref.3

Mutagenesis

159

1

R → A: Strongly reduces enzyme activity. Ref.1

Mutagenesis

190

1

H → A: Strongly reduces enzyme activity. Ref.3

Secondary structure

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295

Helix Strand Turn

Details...

Helix

7 – 16

10

Beta strand

17 – 19

3

Beta strand

21 – 26

6

Helix

29 – 38

10

Beta strand

43 – 45

3

Helix

48 – 52

5

Turn

58 – 60

3

Helix

65 – 76

12

Beta strand

82 – 85

4

Beta strand

90 – 92

3

Helix

93 – 105

13

Beta strand

110 – 114

5

Beta strand

126 – 128

3

Helix

135 – 148

14

Beta strand

155 – 160

6

Turn

162 – 166

5

Helix

169 – 181

13

Beta strand

185 – 189

5

Beta strand

193 – 196

4

Helix

197 – 206

10

Beta strand

208 – 210

3

Beta strand

212 – 214

3

Turn

218 – 221

4

Helix

224 – 230

7

Beta strand

234 – 237

4

Helix

240 – 259

20

Beta strand

260 – 262

3

Turn

263 – 265

3

Helix

266 – 268

3

Helix

272 – 277

6

Helix

281 – 291

11

Sequences

	Sequence		Length	Mass (Da)
	P56839 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A8A7CC4FD6B031F8	FASTA	295	32,912
	10 20 30 40 50 60 MSTKVKKTTQ LKQMLNSKDL EFIMEAHNGL SARIVQEAGF KGIWGSGLSV SAQLGVRDSN 70 80 90 100 110 120 EASWTQVVEV LEFMSDASDV PILLDADTGY GNFNNARRLV RKLEDRGVAG ACLEDKLFPK 130 140 150 160 170 180 TNSLHDGRAQ PLADIEEFAL KIKACKDSQT DPDFCIVARV EAFIAGWGLD EALKRAEAYR 190 200 210 220 230 240 NAGADAILMH SKKADPSDIE AFMKAWNNQG PVVIVPTKYY KTPTDHFRDM GVSMVIWANH 250 260 270 280 290 NLRASVSAIQ QTTKQIYDDQ SLVNVEDKIV SVKEIFRLQR DDELVQAEDK YLPKN

References

[1]	"Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues." Jia Y., Lu Z., Huang K., Herzberg O., Dunaway-Mariano D. Biochemistry 38:14165-14173(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16 AND 115-129, MUTAGENESIS OF ASP-58; ASP-85; ASP-87; GLU-114 AND ARG-159, HOMOTETRAMERIZATION.
[2]	"Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate." Huang K., Li Z., Jia Y., Dunaway-Mariano D., Herzberg O. Structure 7:539-548(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MG(2+) AND AN OXALATE INHIBITOR, HOMOTETRAMERIZATION.
[3]	"Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants." Liu S., Lu Z., Jia Y., Dunaway-Mariano D., Herzberg O. Biochemistry 41:10270-10276(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 6-295 IN COMPLEX WITH SULFOPYRUVATE, MUTAGENESIS OF ASP-58; ASN-122 AND HIS-190.
+	Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M1B	X-ray	2.25	A/B	1-295	[»]
1PYM	X-ray	1.80	A/B	1-295	[»]
1S2T	X-ray	2.00	A/B	1-295	[»]
1S2U	X-ray	2.00	A/B	1-295	[»]
1S2V	X-ray	2.10	A/B/C/D	1-295	[»]
1S2W	X-ray	1.69	A	1-295	[»]

ProteinModelPortal

P56839.

SMR

P56839. Positions 5-295.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16744.

UniPathway

UPA00960.

Family and domain databases

Gene3D

3.20.20.60. 1 hit.

InterPro

IPR012698. PEnolPyrv_PMutase_core.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]

SUPFAM

SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.

TIGRFAMs

TIGR02320. PEP_mutase. 1 hit.

PROSITE

PS00161. ISOCITRATE_LYASE. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P56839.

Entry information

Entry name

PEPM_MYTED

Accession

Primary (citable) accession number: P56839

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)