Reviewed, UniProtKB/Swiss-Prot Q884P1 (MTNC_PSESM)

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:	PSPTO_2047

Organism

Pseudomonas syringae pv. tomato [Complete proteome] [HAMAP]

Taxonomic identifier

323 [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 biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP 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: HAMAP 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity Inferred from electronic annotation. Source: HAMAP acireductone synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: HAMAP 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_0000357393

Sequences

	Sequence		Length	Mass (Da)
	Q884P1-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 055CC48F3F40B52B	FASTA	227	24,671
	10 20 30 40 50 60 MPIKAILTDI EGTTSAVSFV FDVLFPFARA HLPDFVRQHA EQPQVAAQLQ AVRTQSAEPD 70 80 90 100 110 120 ADVERVIAIL LEWIAEDRKA TPLKALQGMV WEQGYNAGQL KGHVYPDAVD ALQHWHQQGY 130 140 150 160 170 180 RLFVYSSGSI QAQQLIFGCS EAGDLSGLFS GYFDTTSGPK REAQSYQTIA NATGFAAEEI 190 200 210 220 LFLSDIVEEL DAAKAAGMLT CGLARDGGVL AGHRHVNSFT LIDPASF

References

[1]

"The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000." Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C., Davidsen T.M., Zafar N. , Zhou L., Liu J., Yuan Q., Khouri H.M., Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R., Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R., Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G., Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., Collmer A. Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003) [PubMed: 12928499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DC3000.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016853 Genomic DNA. Translation: AAO55565.1.
RefSeq	NP_791870.1.
3D structure databases
HSSP	HSSP built from PDB template 2G80 based on UniProtKB P32626.
SMR	Q884P1. Positions 2-223.
ModBase	Search...
Genome annotation databases
GeneID	1183692.
GenomeReviews	Gene locus PSPTO_2047 in contig AE016853_GR.
KEGG	pst:PSPTO_2047.
NMPDR	fig|223283.1.peg.2008.
TIGR	PSPTO2047.
Phylogenomic databases
HOGENOM	HBG294242.
OMA	TTDLNFI.
Enzyme and pathway databases
BioCyc	PSYR223283:PSPTO_2047-MONOMER.
Family and domain databases
HAMAP	MF_01681. Salvage_MtnC. [Tree]
InterPro	IPR005834. Dehalogen-like_hydro. IPR010041. Enolase_ppase. IPR006439. HAD-SF_hydro_IA_v1. [Graphical view]
PANTHER	PTHR20371. Enolase_ppase. 1 hit.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01691. enolase-ppase. 1 hit. TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTNC_PSESM

Accession

Primary (citable) accession number: Q884P1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)