Q48KM6 (MTNC_PSE14) 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:	PSPPH_1816

Organism

Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]

Taxonomic identifier

264730 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas syringae pv. savastanoi

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_0000357391

Sequences

	Sequence		Length	Mass (Da)
	Q48KM6 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: BA63D2B95C54B63B	FASTA	227	24,583
	10 20 30 40 50 60 MPIKAILTDI EGTTSAVSFV FDVLFPFAKK HLPGFVRQNA GQPAVASQLQ AVRTEAGEPD 70 80 90 100 110 120 ADVERVIAIL LEWIAEDRKA TPLKALQGMV WEQGYNAGQL KGHVYPDAVD ALKHWHQQGY 130 140 150 160 170 180 RLYVYSSGSI QAQQLIFGCS EAGDLSGLFS GYFDTTSGPK REAQSYRTIA QAIECPAENI 190 200 210 220 LFLSDIVEEL DAAQAAGMIT CGLARDGGVL VGHRYVSSFA LIDPASF

References

[1]

"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition." Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R. J. Bacteriol. 187:6488-6498(2005) [PubMed: 16159782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1448A / Race 6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000058 Genomic DNA. Translation: AAZ37666.1.
RefSeq	YP_274049.1. NC_005773.3.
3D structure databases
HSSP	HSSP built from PDB template 2G80 based on UniProtKB P32626.
ProteinModelPortal	Q48KM6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q48KM6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3560328.
GenomeReviews	Gene locus PSPPH_1816 in contig CP000058_GR.
KEGG	psp:PSPPH_1816.
NMPDR	fig|264730.3.peg.1921.
PATRIC	19972824. VBIPseSyr78478_1907.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4229.
HOGENOM	HBG294242.
OMA	TTDLNFI.
PhylomeDB	Q48KM6.
ProtClustDB	CLSK866737.
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_PSE14

Accession

Primary (citable) accession number: Q48KM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	September 13, 2005
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program