Q8EKK8 (MTNC_SHEON) 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:	SO_0084

Organism

Shewanella oneidensis

Taxonomic identifier

70863 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	226 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 Reference 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 – 226	226	Enolase-phosphatase E1 HAMAP MF_01681		PRO_0000357404

Sequences

	Sequence		Length	Mass (Da)
	Q8EKK8 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: B8D4597116D41D15	FASTA	226	25,472
	10 20 30 40 50 60 MGIRAIVVDT AGTTTDLTFI QDVLFPYSVK ALPDFLAQNQ HNVLVENCIC DTRDIALEPD 70 80 90 100 110 120 ADLNRVTEIL QQWVREDRKA TPLKTLQGLI WKQGYAHDEF KGHIFPDFIE AVKRFSAQNL 130 140 150 160 170 180 RIYSFSSGSV DAQKLLFSHS DGGDLTEMFN GHFDTRTGNK LDKQAYCNIL NTISLSPKQV 190 200 210 220 LFVSDVIEEL KAADAAGMMT CQMVRDSKQR TGDFRTINSF DKLVIE

References

[1]

"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis." Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M. Nat. Biotechnol. 20:1118-1123(2002) [PubMed: 12368813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MR-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014299 Genomic DNA. Translation: AAN53171.1.
RefSeq	NP_715726.1. NC_004347.1.
3D structure databases
HSSP	HSSP built from PDB template 1ZS9 based on UniProtKB Q9UHY7.
ProteinModelPortal	Q8EKK8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1167982.
GenomeReviews	Gene locus SO_0084 in contig AE014299_GR.
KEGG	son:SO_0084.
NMPDR	fig|211586.1.peg.84.
PATRIC	23519869. VBISheOne101494_0085.
TIGR	SO_0084.
Phylogenomic databases
HOGENOM	HBG294242.
OMA	TTDLNFI.
ProtClustDB	CLSK866737.
Enzyme and pathway databases
BioCyc	SONE211586:SO_0084-MONOMER.
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_SHEON

Accession

Primary (citable) accession number: Q8EKK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program