Q3KFI7 (MTNC_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase-phosphatase E1
EC=3.1.3.77

Alternative name(s):
2,3-diketo-5-methylthio-1-phosphopentane phosphatase

Gene names

Name:	mtnC
Ordered Locus Names:	Pfl01_1726

Organism

Pseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]

Taxonomic identifier

205922 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) By similarity. HAMAP MF_01681
Catalytic activity	5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate. HAMAP MF_01681
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01681
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6. HAMAP MF_01681 Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6.
Subunit structure	Monomer By similarity. HAMAP MF_01681
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. MasA/mtnC family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-methionine salvage from methylthioadenosine Inferred from electronic annotation. Source: InterPro
Molecular function	2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity Inferred from electronic annotation. Source: InterPro 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity Inferred from electronic annotation. Source: InterPro acireductone synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglycolate phosphatase activity 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 – 227	227	Enolase-phosphatase E1 HAMAP MF_01681		PRO_0000357390

Sequences

	Sequence		Length	Mass (Da)
	Q3KFI7 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: B6795BEEF90E38AA	FASTA	227	24,939
	10 20 30 40 50 60 MSIKVILTDI EGTTSAVSFV FDVLFPYAAK HLPDFVRQNA QRADVAEQLD AVRRDSNEPQ 70 80 90 100 110 120 ADVERVVEIL LAWIAEDRKA TPLKALQGMV WEQGYQAGQL KGHVYPDAVE ALQRWHQAGY 130 140 150 160 170 180 QLFVYSSGSI QAQKLIFGCS EAGDLTPLFS GYFDTTSGPK REPQSYTNIQ QAIGVEPQEI 190 200 210 220 LFLSDIVQEL DAAQSAGLQT CGLAREGGEL EGHVTVDSFT GIEPEAF

References

[1]

"Genomic and genetic analyses of diversity and plant interactions of Pseudomonas fluorescens." Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., Harris S., Challis G.L., Yaxley A.M., Harris D. , Seeger K., Murphy L., Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., Parkhill J., Levy S.B., Rainey P.B., Thomson N.R. Genome Biol. 10:R51.1-R51.16(2009) [PubMed: 19432983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pf0-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000094 Genomic DNA. Translation: ABA73469.1.
RefSeq	YP_347458.1. NC_007492.2.
3D structure databases
HSSP	HSSP built from PDB template 2G80 based on UniProtKB P32626.
ProteinModelPortal	Q3KFI7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3KFI7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3716677.
GenomeReviews	Gene locus Pfl01_1726 in contig CP000094_GR.
KEGG	pfo:Pfl01_1726.
PATRIC	19885571. VBIPseFlu44242_1755.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4229.
HOGENOM	HBG294242.
OMA	TTDLNFI.
ProtClustDB	CLSK866737.
Enzyme and pathway databases
BioCyc	PFLU205922:PFL_1726-MONOMER.
Family and domain databases
HAMAP	MF_01681. Salvage_MtnC. [Tree]
InterPro	IPR005834. Dehalogen-like_hydro. IPR023943. Enolase-phosphatase_E1. IPR010041. Enolase_ppase. IPR023214. HAD-like_dom. IPR006439. HAD-SF_hydro_IA_v1. IPR005833. Haloacid_DH/epoxide_hydro. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K09880.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00413. HADHALOGNASE.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01691. Enolase-ppase. 1 hit. TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTNC_PSEPF

Accession

Primary (citable) accession number: Q3KFI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 8, 2005
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program