Q04QY0 (MTNC_LEPBJ) 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:	LBJ_2207

Organism

Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Complete proteome] [HAMAP]

Taxonomic identifier

355277 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	231 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 – 231	231	Enolase-phosphatase E1 HAMAP MF_01681		PRO_0000357377

Sequences

	Sequence		Length	Mass (Da)
	Q04QY0 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 4FD2834D3BF49F21	FASTA	231	26,452
	10 20 30 40 50 60 MDFEIYLFDI EGTTTPIEFV HKILFPYSVG KFETFFRSNS LERKWIEKLL EEGKRDSTYS 70 80 90 100 110 120 RQLTDSPQNL SDYCKYLVSV DRKSGPLKEI QGRIWKHGYE NGELKSSLFA DVPSFLKRIQ 130 140 150 160 170 180 SAKKKSAVYS SGSIEAQKLI FKYSDFGDLT EYFSAYFDTG VGGKRESASY SRIAEQLGIA 190 200 210 220 230 PEKILFFTDI KEEADAARNA EFKTTLLERP GNAPQPKHSH PKISSFENFN P

References

[1]

"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential." Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B. Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed: 16973745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JB197.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000350 Genomic DNA. Translation: ABJ76690.1.
RefSeq	YP_801448.1. NC_008510.1.
3D structure databases
ProteinModelPortal	Q04QY0.
ModBase	Search...
Protein-protein interaction databases
STRING	Q04QY0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4411643.
GenomeReviews	Gene locus LBJ_2207 in contig CP000350_GR.
KEGG	lbj:LBJ_2207.
PATRIC	22360248. VBILepBor13265_2828.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4229.
HOGENOM	HBG294242.
OMA	TTDLNFI.
PhylomeDB	Q04QY0.
ProtClustDB	CLSK866737.
Enzyme and pathway databases
BioCyc	LBOR355277:LBJ_2207-MONOMER.
Family and domain databases
HAMAP	MF_01681. Salvage_MtnC. [Tree]
InterPro	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.
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_LEPBJ

Accession

Primary (citable) accession number: Q04QY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program