Q0BPT7 (MTNC_GRABC) 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:	GbCGDNIH1_2267

Organism

Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP]

Taxonomic identifier

391165 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Granulibacter

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_0000357369

Sequences

	Sequence		Length	Mass (Da)
	Q0BPT7 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 13E3B30247EBF479	FASTA	231	25,127
	10 20 30 40 50 60 MNPPKAILTD IEGTTTPIAF VHRVLFPYAK ANMAGFLAAY SDDEAVAAIL AEVEAQYPGR 70 80 90 100 110 120 PALETLLGWM DEDAKITPLK ALQGLIWREG YRNGALQAQV HPDAAQSLRA WHEAGLNLFV 130 140 150 160 170 180 YSSGSVEAQQ LLFSYSDQGD LSLLFGGFFD TRIGGKREAD SYRHIIANTG MQPQSMLFLS 190 200 210 220 230 DIEEELDAAL DAGLRTCQLV RAGDNGGPPT LRHPHAPDFI AVAHLFGLPH P

References

[1]

"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis." Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M. J. Bacteriol. 189:8727-8736(2007) [PubMed: 17827295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-1260 / CGDNIH1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000394 Genomic DNA. Translation: ABI63165.1.
RefSeq	YP_746088.1. NC_008343.1.
3D structure databases
ProteinModelPortal	Q0BPT7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0BPT7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4276031.
GenomeReviews	Gene locus GbCGDNIH1_2267 in contig CP000394_GR.
KEGG	gbe:GbCGDNIH1_2267.
NMPDR	fig|391165.8.peg.2202.
PATRIC	22080805. VBIGraBet83793_2351.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4229.
HOGENOM	HBG294242.
OMA	TTDLNFI.
PhylomeDB	Q0BPT7.
ProtClustDB	CLSK866737.
Enzyme and pathway databases
BioCyc	GBET391165:GBCGDNIH1_2267-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. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.
KO	K09880.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
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_GRABC

Accession

Primary (citable) accession number: Q0BPT7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program