Reviewed, UniProtKB/Swiss-Prot Q60AP9 (MTNC_METCA)

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:	MCA0797

Organism

Methylococcus capsulatus [Complete proteome] [HAMAP]

Taxonomic identifier

414 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus

Protein attributes

Sequence length	227 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 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 – 227	227	Enolase-phosphatase E1 HAMAP MF_01681		PRO_0000357382

Sequences

	Sequence		Length	Mass (Da)
	Q60AP9-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: 43CD11C20F73C07E	FASTA	227	25,246
	10 20 30 40 50 60 MIRAILTDIE GTTSSLSFVK ETLFPYARAR MADFVRGHAR DATVQALLAD AKAAAGDPSM 70 80 90 100 110 120 DDEHVIARLV RWIDEDRKIT PLKALQGLIW EEGYRNRDFF GHVYDDAVRR LKAWHEQGIS 130 140 150 160 170 180 LYVFSSGSVH AQRLLFGHTA AGDLQPLFSG YFDTRIGAKQ EPAAYSAIAR ELNLPPSEIL 190 200 210 220 FLSDIEAELD AAREAGYKTF MLVREGGAKA SHHPQGADFD AIRPELL

References

[1]

"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. , Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L., Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H., Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R., Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A. PLoS Biol. 2:1616-1628(2004) [PubMed: 15383840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bath / NCIMB 11132.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017282 Genomic DNA. Translation: AAU92902.1.
RefSeq	YP_113298.1.
3D structure databases
HSSP	HSSP built from PDB template 2G80 based on UniProtKB P32626.
SMR	Q60AP9. Positions 2-212.
ModBase	Search...
Genome annotation databases
GeneID	3103415.
GenomeReviews	Gene locus MCA0797 in contig AE017282_GR.
KEGG	mca:MCA0797.
NMPDR	fig|243233.4.peg.1588.
TIGR	MCA0797.
Phylogenomic databases
HOGENOM	HBG294242.
OMA	TTDLNFI.
Enzyme and pathway databases
BioCyc	MCAP243233:MCA_0797-MONOMER.
Family and domain databases
HAMAP	MF_01681. Salvage_MtnC. [Tree]
InterPro	IPR005834. Dehalogen-like_hydro. IPR010041. Enolase_ppase. IPR006439. HAD-SF_hydro_IA_v1. [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.
ProtoNet	Search...

Entry information

Entry name

MTNC_METCA

Accession

Primary (citable) accession number: Q60AP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 23, 2004
Last modified:	February 9, 2010
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)