Q72NW0 (MTNC_LEPIC) 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:	LIC_12718

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]

Taxonomic identifier

267671 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

Protein attributes

Sequence length	234 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 234	234	Enolase-phosphatase E1 HAMAP MF_01681		PRO_0000357380

Sequences

	Sequence		Length	Mass (Da)
	Q72NW0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: F5C2A87D9190FE0C	FASTA	234	26,678
	10 20 30 40 50 60 MNIKTFEFYL FDIEGTTTPI EFVHKILFPY SVEKFDSFFQ SNLLEKEWIE KLILEGKNDT 70 80 90 100 110 120 TYSGKLSDSA FDLSEYCKHL VSLDRKSGIL KEIQGRIWKS GYENGELKSS MFSDVPSFLK 130 140 150 160 170 180 KIQASKKKSA VYSSGSIQAQ KLIFEYSDFG NLTHFFYAYF DTGVGGKRES SSYSKISEQL 190 200 210 220 230 GVAPEKILFF TDIKEEADAA KEAKLHSAIL ERPGNYPQPQ HSHFKISSFE GLNP

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed: 15028702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016823 Genomic DNA. Translation: AAS71276.1.
RefSeq	YP_002639.1. NC_005823.1.
3D structure databases
HSSP	HSSP built from PDB template 2G80 based on UniProtKB P32626.
ProteinModelPortal	Q72NW0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2770784.
GenomeReviews	Gene locus LIC_12718 in contig AE016823_GR.
KEGG	lic:LIC12718.
PATRIC	22378223. VBILepInt6257_3265.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG294242.
OMA	TTDLNFI.
PhylomeDB	Q72NW0.
ProtClustDB	CLSK866737.
Enzyme and pathway databases
BioCyc	LINT267671:LIC_12718-MONOMER.
Family and domain databases
HAMAP	MF_01681. Salvage_MtnC. [Tree]
InterPro	IPR023943. Enolase-phosphatase_E1. IPR010041. Enolase_ppase. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K09880.
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01691. Enolase-ppase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTNC_LEPIC

Accession

Primary (citable) accession number: Q72NW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program