Q7V8Y7 (MTNC_PROMM) 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:	PMT_0184

Organism

Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]

Taxonomic identifier

74547 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	245 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 – 245	245	Enolase-phosphatase E1 HAMAP MF_01681		PRO_0000357386

Sequences

	Sequence		Length	Mass (Da)
	Q7V8Y7 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 5ADC8EDA6B3B1BEF	FASTA	245	27,913
	10 20 30 40 50 60 MITHILLDIE GTTCPTSFVS DTLFPYADTH LEGFLNEHIE NNEVQSLIDE AWHEWQADED 70 80 90 100 110 120 PSSKDLLSKA FRENSSEIEN ICSYLHHLIT IDRKSSALKD LQGRIWREGY EKGDISSSLY 130 140 150 160 170 180 PETIEVLNKL KQQDYILAVY SSGSISAQKL LYRHTTNGDQ TALFSHWFDT RTGNKKESKS 190 200 210 220 230 240 YSDISIAMNI PVEKVMFVSD SCAECNAAKK AGMSVLFSLR EGNPEQDPHD HQPIKDLRCL FDYLL

References

[1]

"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W. Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MIT 9313.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX548175 Genomic DNA. Translation: CAE20359.1.
RefSeq	NP_894017.1. NC_005071.1.
3D structure databases
HSSP	HSSP built from PDB template 2G80 based on UniProtKB P32626.
ProteinModelPortal	Q7V8Y7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7V8Y7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1729665.
GenomeReviews	Gene locus PMT_0184 in contig BX548175_GR.
KEGG	pmt:PMT0184.
NMPDR	fig|74547.1.peg.184.
PATRIC	23008073. VBIProMar135351_0199.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4229.
HOGENOM	HBG294242.
OMA	TTDLNFI.
PhylomeDB	Q7V8Y7.
ProtClustDB	CLSK866737.
Enzyme and pathway databases
BioCyc	PMAR74547:PMT0184-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. [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.
ProtoNet	Search...

Entry information

Entry name

MTNC_PROMM

Accession

Primary (citable) accession number: Q7V8Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program