Reviewed, UniProtKB/Swiss-Prot Q8P9N5 (MTNC_XANCP)

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:	XCC1818

Organism

Xanthomonas campestris pv. campestris [Complete proteome] [HAMAP]

Taxonomic identifier

340 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	232 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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.
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	methionine biosynthetic process from S-adenosylmethionine Inferred from electronic annotation. Source: HAMAP methionine salvage 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 – 232	232	Enolase-phosphatase E1 HAMAP MF_01681		PRO_0000357428

Sequences

	Sequence		Length	Mass (Da)
	Q8P9N5-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 38BFD0A622968609	FASTA	232	26,013
	10 20 30 40 50 60 MTRPQAILTD IEGTTSSISF VKDVLFPYAR RAMPAYVREH GGHPQVRHWL NQVADEIGED 70 80 90 100 110 120 VPDEVLITTL QTWIDEDRKH TALKALQGMI WEDGYRTADF SAHIYTDAAI QLQAWHAEGI 130 140 150 160 170 180 PLYVYSSGSV PAQKLFFAHS DAGDLSGLVS DWFDTEVGPK RESSSYRRIA ERIGVPAPEI 190 200 210 220 230 LFLSDVIEEL DAAKRAGMRT ALLDRLEDYP TPRSADDVGS HQRVESFTQL VL

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008922 Genomic DNA. Translation: AAM41107.1.
RefSeq	NP_637183.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	998471.
GenomeReviews	Gene locus XCC1818 in contig AE008922_GR.
KEGG	xcc:XCC1818.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8P9N5.
OMA	TTDLNFI.
Enzyme and pathway databases
BioCyc	XCAM190485:XCC1818-MON.
Family and domain databases
HAMAP	MF_01681. [Tree]
InterPro	IPR005834. Dehalogen-like_hydro. IPR010041. Enolase_ppase. IPR006439. HAD-SF_hydro_IA_v1. IPR006402. HAD-SF_hydro_IA_v3. [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. TIGR01509. HAD-SF-IA-v3. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTNC_XANCP

Accession

Primary (citable) accession number: Q8P9N5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 1, 2002
Last modified:	November 3, 2009
This is version 38 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)