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Q8BGB7 (ENOPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enolase-phosphatase E1

EC=3.1.3.77
Alternative name(s):
2,3-diketo-5-methylthio-1-phosphopentane phosphatase
MASA homolog
Gene names
Name:Enoph1
Synonyms:Masa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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-Rule MF_03117

Catalytic activity

5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate. HAMAP-Rule MF_03117

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_03117

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-Rule MF_03117

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-Rule MF_03117

Subcellular location

Cytoplasm By similarity. Nucleus By similarity HAMAP-Rule MF_03117.

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.

Sequence caution

The sequence BAE30883.1 differs from that shown. Reason: Frameshift at position 220.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BGB7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BGB7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     55-85: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257Enolase-phosphatase E1 HAMAP-Rule MF_03117
PRO_0000254008

Regions

Region150 – 1512Substrate binding By similarity

Sites

Metal binding161Magnesium By similarity
Metal binding181Magnesium; via carbonyl oxygen By similarity
Metal binding2091Magnesium By similarity
Binding site1841Substrate By similarity

Natural variations

Alternative sequence55 – 8531Missing in isoform 2.
VSP_021161

Experimental info

Sequence conflict561V → I in AAH21429. Ref.2
Sequence conflict741P → L in AAH21429. Ref.2
Sequence conflict1521G → R in BAB26606. Ref.1
Sequence conflict2361T → N in BAE35014. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: AD64B1C70976C344

FASTA25728,600
        10         20         30         40         50         60 
MVVVSVPAEV TVILLDIEGT TTPIAFVKDV LFPYIKENVK EYLQTHWEEE ECQQDVSLLR 

        70         80         90        100        110        120 
KQAEEDAHLD GAVPIPVASG SDLQQMIQAV VDNVYWQMSH DRKTTALKQL QGHMWKAAFT 

       130        140        150        160        170        180 
AGRMKAEFFA DVVPAVRRWR EAGMKVYIYS SGSVEAQKLL FGHSTEGDIL ELIDGHFDTK 

       190        200        210        220        230        240 
IGHKVDSESY RKIADSIGCS TNNILFLTDV TVEASAAEEA DVHVAVVVRP GNAGLTDDEK 

       250 
TYYNLITSFS ELYLPST 

« Hide

Isoform 2 [UniParc].

Checksum: C8DBC7513DB08943
Show »

FASTA22625,359

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Bone marrow macrophage, Diencephalon, Embryonic kidney, Osteoclast, Placenta, Retina and Tongue.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009954 mRNA. Translation: BAB26606.1.
AK079062 mRNA. Translation: BAC37520.1.
AK080714 mRNA. Translation: BAC37988.1.
AK082747 mRNA. Translation: BAC38597.1.
AK152021 mRNA. Translation: BAE30883.1. Frameshift.
AK159356 mRNA. Translation: BAE35014.1.
AK167575 mRNA. Translation: BAE39638.1.
AK168696 mRNA. Translation: BAE40540.1.
BC021429 mRNA. Translation: AAH21429.1.
RefSeqNP_001156507.1. NM_001163035.1.
NP_080697.2. NM_026421.3.
UniGeneMm.11311.

3D structure databases

ProteinModelPortalQ8BGB7.
SMRQ8BGB7. Positions 4-254.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212497. 1 interaction.
IntActQ8BGB7. 1 interaction.
MINTMINT-4110231.
STRING10090.ENSMUSP00000031268.

Proteomic databases

PaxDbQ8BGB7.
PRIDEQ8BGB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031268; ENSMUSP00000031268; ENSMUSG00000029326. [Q8BGB7-1]
ENSMUST00000169390; ENSMUSP00000129704; ENSMUSG00000029326. [Q8BGB7-1]
GeneID67870.
KEGGmmu:67870.
UCSCuc008yha.2. mouse. [Q8BGB7-1]

Organism-specific databases

CTD58478.
MGIMGI:1915120. Enoph1.

Phylogenomic databases

eggNOGCOG4229.
GeneTreeENSGT00440000039914.
HOGENOMHOG000237286.
HOVERGENHBG054539.
InParanoidQ8BGB7.
KOK09880.
OMADTHVGHK.
OrthoDBEOG7BP83J.
PhylomeDBQ8BGB7.
TreeFamTF105939.

Enzyme and pathway databases

UniPathwayUPA00904; UER00876.
UPA00904; UER00877.

Gene expression databases

BgeeQ8BGB7.
CleanExMM_ENOPH1.
GenevestigatorQ8BGB7.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
HAMAPMF_01681. Salvage_MtnC.
MF_03117. Salvage_MtnC_euk.
InterProIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
[Graphical view]
PfamPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSENOPH1. mouse.
NextBio325783.
PROQ8BGB7.
SOURCESearch...

Entry information

Entry nameENOPH_MOUSE
AccessionPrimary (citable) accession number: Q8BGB7
Secondary accession number(s): Q3TGK8 expand/collapse secondary AC list , Q3TXA2, Q3U8Y4, Q8VC92, Q9D6U4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot