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Protein

Enolase-phosphatase E1

Gene

Enoph1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).UniRule annotation

Catalytic activityi

5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathway: L-methionine biosynthesis via salvage pathway

This protein is involved in step 3 and 4 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (Mri1)
  2. Methylthioribulose-1-phosphate dehydratase (Apip)
  3. Enolase-phosphatase E1 (Enoph1)
  4. Enolase-phosphatase E1 (Enoph1)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1)
  6. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161MagnesiumUniRule annotation
Metal bindingi18 – 181Magnesium; via carbonyl oxygenUniRule annotation
Binding sitei184 – 1841SubstrateUniRule annotation
Metal bindingi209 – 2091MagnesiumUniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_310863. Methionine salvage pathway.
UniPathwayiUPA00904; UER00876.
UPA00904; UER00877.

Names & Taxonomyi

Protein namesi
Recommended name:
Enolase-phosphatase E1UniRule annotation (EC:3.1.3.77UniRule annotation)
Alternative name(s):
2,3-diketo-5-methylthio-1-phosphopentane phosphataseUniRule annotation
MASA homologUniRule annotation
Gene namesi
Name:Enoph1
Synonyms:Masa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1915120. Enoph1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Enolase-phosphatase E1PRO_0000254008Add
BLAST

Proteomic databases

MaxQBiQ8BGB7.
PaxDbiQ8BGB7.
PRIDEiQ8BGB7.

Expressioni

Gene expression databases

BgeeiQ8BGB7.
CleanExiMM_ENOPH1.
GenevisibleiQ8BGB7. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi212497. 1 interaction.
IntActiQ8BGB7. 1 interaction.
MINTiMINT-4110231.
STRINGi10090.ENSMUSP00000031268.

Structurei

3D structure databases

ProteinModelPortaliQ8BGB7.
SMRiQ8BGB7. Positions 4-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 1512Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG4229.
GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
HOVERGENiHBG054539.
InParanoidiQ8BGB7.
KOiK09880.
OMAiIKGEVYQ.
OrthoDBiEOG7BP83J.
PhylomeDBiQ8BGB7.
TreeFamiTF105939.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_01681. Salvage_MtnC.
MF_03117. Salvage_MtnC_euk.
InterProiIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BGB7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVVVSVPAEV TVILLDIEGT TTPIAFVKDV LFPYIKENVK EYLQTHWEEE
60 70 80 90 100
ECQQDVSLLR KQAEEDAHLD GAVPIPVASG SDLQQMIQAV VDNVYWQMSH
110 120 130 140 150
DRKTTALKQL QGHMWKAAFT AGRMKAEFFA DVVPAVRRWR EAGMKVYIYS
160 170 180 190 200
SGSVEAQKLL FGHSTEGDIL ELIDGHFDTK IGHKVDSESY RKIADSIGCS
210 220 230 240 250
TNNILFLTDV TVEASAAEEA DVHVAVVVRP GNAGLTDDEK TYYNLITSFS

ELYLPST
Length:257
Mass (Da):28,600
Last modified:March 1, 2003 - v1
Checksum:iAD64B1C70976C344
GO
Isoform 2 (identifier: Q8BGB7-2) [UniParc]FASTAAdd to basket

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

Show »
Length:226
Mass (Da):25,359
Checksum:iC8DBC7513DB08943
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561V → I in AAH21429 (PubMed:15489334).Curated
Sequence conflicti74 – 741P → L in AAH21429 (PubMed:15489334).Curated
Sequence conflicti152 – 1521G → R in BAB26606 (PubMed:16141072).Curated
Sequence conflicti236 – 2361T → N in BAE35014 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 8531Missing in isoform 2. 1 PublicationVSP_021161Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39183.1. [Q8BGB7-1]
RefSeqiNP_001156507.1. NM_001163035.1. [Q8BGB7-1]
NP_080697.2. NM_026421.3. [Q8BGB7-1]
UniGeneiMm.11311.

Genome annotation databases

EnsembliENSMUST00000031268; ENSMUSP00000031268; ENSMUSG00000029326. [Q8BGB7-1]
ENSMUST00000169390; ENSMUSP00000129704; ENSMUSG00000029326. [Q8BGB7-1]
GeneIDi67870.
KEGGimmu:67870.
UCSCiuc008yha.2. mouse. [Q8BGB7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39183.1. [Q8BGB7-1]
RefSeqiNP_001156507.1. NM_001163035.1. [Q8BGB7-1]
NP_080697.2. NM_026421.3. [Q8BGB7-1]
UniGeneiMm.11311.

3D structure databases

ProteinModelPortaliQ8BGB7.
SMRiQ8BGB7. Positions 4-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212497. 1 interaction.
IntActiQ8BGB7. 1 interaction.
MINTiMINT-4110231.
STRINGi10090.ENSMUSP00000031268.

Proteomic databases

MaxQBiQ8BGB7.
PaxDbiQ8BGB7.
PRIDEiQ8BGB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031268; ENSMUSP00000031268; ENSMUSG00000029326. [Q8BGB7-1]
ENSMUST00000169390; ENSMUSP00000129704; ENSMUSG00000029326. [Q8BGB7-1]
GeneIDi67870.
KEGGimmu:67870.
UCSCiuc008yha.2. mouse. [Q8BGB7-1]

Organism-specific databases

CTDi58478.
MGIiMGI:1915120. Enoph1.

Phylogenomic databases

eggNOGiCOG4229.
GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
HOVERGENiHBG054539.
InParanoidiQ8BGB7.
KOiK09880.
OMAiIKGEVYQ.
OrthoDBiEOG7BP83J.
PhylomeDBiQ8BGB7.
TreeFamiTF105939.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00876.
UPA00904; UER00877.
ReactomeiREACT_310863. Methionine salvage pathway.

Miscellaneous databases

ChiTaRSiEnoph1. mouse.
NextBioi325783.
PROiQ8BGB7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGB7.
CleanExiMM_ENOPH1.
GenevisibleiQ8BGB7. MM.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
HAMAPiMF_01681. Salvage_MtnC.
MF_03117. Salvage_MtnC_euk.
InterProiIPR023943. Enolase-ppase_E1.
IPR027511. ENOPH1_eukaryotes.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiENOPH_MOUSE
AccessioniPrimary (citable) accession number: Q8BGB7
Secondary accession number(s): Q3TGK8
, Q3TXA2, Q3U8Y4, Q8VC92, Q9D6U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.