Reviewed, UniProtKB/Swiss-Prot Q0VPK3 (MTNC_ALCBS)

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:	ABO_1447

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

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
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
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_0000357357

Sequences

	Sequence		Length	Mass (Da)
	Q0VPK3-1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 31CD664BD6FF7FD6	FASTA	226	24,974
	10 20 30 40 50 60 MINAIITDIE GTTSSIAFVK EVLFPYAAKR FPDFLADHWD HPCVQEQIKA AEKESGETLG 70 80 90 100 110 120 SADKAAALFL RWIEEDRKAT PLKTLQGMIW KAGYENGDYT AHMYPDTAPA LKKWHQKGIA 130 140 150 160 170 180 LYVYSSGSIT AQKLFFGYSD AGDLTGLLSG YFDTTTGPKQ ETDSYRKIQQ AIDKPANTLL 190 200 210 220 FLSDIEAELD AAAEAGFNTC LLDRQQAGLE SRHPVASNFN HINLAD

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL16895.1. Different initiation.
RefSeq	YP_693167.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VPK3.
Genome annotation databases
GeneID	4212624.
GenomeReviews	Gene locus ABO_1447 in contig AM286690_GR.
KEGG	abo:ABO_1447.
NMPDR	fig|393595.12.peg.1453.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4229.
HOGENOM	HBG294242.
PhylomeDB	Q0VPK3.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1447-MONOMER.
Family and domain databases
HAMAP	MF_01681. Salvage_MtnC. [Tree]
InterPro	IPR005834. Dehalogen-like_hydro. IPR010041. Enolase_ppase. IPR005833. Haloacid_DH/epoxide_hydro. [Graphical view]
PANTHER	PTHR20371. Enolase_ppase. 1 hit.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00413. HADHALOGNASE.
TIGRFAMs	TIGR01691. enolase-ppase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MTNC_ALCBS

Accession

Primary (citable) accession number: Q0VPK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	December 16, 2008
Last modified:	February 9, 2010
This is version 29 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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