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Protein

Enolase-phosphatase E1

Gene

ENOPH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 annotation1 Publication

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Pathwayi: 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), 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)
  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 annotation1 Publication
Metal bindingi18 – 181Magnesium; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei187 – 1871Substrate
Metal bindingi212 – 2121MagnesiumUniRule annotation1 Publication

GO - Molecular functioni

  • acireductone synthase activity Source: UniProtKB
  • magnesium ion binding Source: InterPro

GO - Biological processi

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.77. 2681.
ReactomeiR-HSA-1237112. 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:ENOPH1UniRule annotation
Synonyms:MASAUniRule annotation
ORF Names:MSTP145
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:24599. ENOPH1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385052.

Polymorphism and mutation databases

BioMutaiENOPH1.
DMDMi74735024.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Enolase-phosphatase E1PRO_0000254007Add
BLAST

Proteomic databases

EPDiQ9UHY7.
MaxQBiQ9UHY7.
PaxDbiQ9UHY7.
PRIDEiQ9UHY7.

PTM databases

DEPODiQ9UHY7.

Expressioni

Gene expression databases

BgeeiQ9UHY7.
CleanExiHS_ENOPH1.
ExpressionAtlasiQ9UHY7. baseline and differential.
GenevisibleiQ9UHY7. HS.

Organism-specific databases

HPAiCAB004985.
HPA044607.
HPA050480.

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi121811. 26 interactions.
IntActiQ9UHY7. 10 interactions.
MINTiMINT-1415620.
STRINGi9606.ENSP00000273920.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154Combined sources
Turni19 – 213Combined sources
Helixi24 – 296Combined sources
Helixi31 – 4616Combined sources
Helixi50 – 6516Combined sources
Turni66 – 683Combined sources
Helixi83 – 10321Combined sources
Helixi108 – 12316Combined sources
Helixi135 – 14410Combined sources
Beta strandi148 – 1525Combined sources
Helixi157 – 1659Combined sources
Helixi173 – 1753Combined sources
Beta strandi177 – 1804Combined sources
Helixi182 – 1843Combined sources
Helixi190 – 20011Combined sources
Helixi204 – 2063Combined sources
Beta strandi207 – 2126Combined sources
Helixi214 – 2229Combined sources
Beta strandi226 – 2305Combined sources
Helixi240 – 2456Combined sources
Beta strandi248 – 2514Combined sources
Helixi252 – 2543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YNSX-ray1.70A1-261[»]
1ZS9X-ray1.70A1-261[»]
ProteinModelPortaliQ9UHY7.
SMRiQ9UHY7. Positions 4-257.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHY7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni153 – 1542Substrate binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2630. Eukaryota.
COG4229. LUCA.
GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
HOVERGENiHBG054539.
InParanoidiQ9UHY7.
KOiK09880.
OMAiPYAKQNV.
OrthoDBiEOG7BP83J.
PhylomeDBiQ9UHY7.
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]
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: Q9UHY7-1) [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
MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE
60 70 80 90 100
ECQQDVSLLR KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ
110 120 130 140 150
MSLDRKTTAL KQLQGHMWRA AFTAGRMKAE FFADVVPAVR KWREAGMKVY
160 170 180 190 200
IYSSGSVEAQ KLLFGHSTEG DILELVDGHF DTKIGHKVES ESYRKIADSI
210 220 230 240 250
GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD DEKTYYSLIT
260
SFSELYLPSS T
Length:261
Mass (Da):28,933
Last modified:May 1, 2000 - v1
Checksum:i12B3F73463907E2C
GO
Isoform 2 (identifier: Q9UHY7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.

Show »
Length:115
Mass (Da):12,552
Checksum:i43E2FD7570657AFC
GO

Sequence cautioni

The sequence AAQ13671.1 differs from that shown. Reason: Frameshift at position 235. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 146146Missing in isoform 2. 1 PublicationVSP_021160Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113125 mRNA. Translation: AAF14866.1.
AK022656 mRNA. Translation: BAB14160.1.
CR457141 mRNA. Translation: CAG33422.1.
BC001317 mRNA. Translation: AAH01317.1.
BC065815 mRNA. Translation: AAH65815.1.
AF177286 mRNA. Translation: AAQ13671.1. Sequence problems.
CCDSiCCDS3594.1. [Q9UHY7-1]
RefSeqiNP_001278946.1. NM_001292017.1.
NP_067027.1. NM_021204.4. [Q9UHY7-1]
UniGeneiHs.18442.

Genome annotation databases

EnsembliENST00000273920; ENSP00000273920; ENSG00000145293. [Q9UHY7-1]
ENST00000505846; ENSP00000427209; ENSG00000145293. [Q9UHY7-2]
GeneIDi58478.
KEGGihsa:58478.
UCSCiuc003hmv.4. human. [Q9UHY7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113125 mRNA. Translation: AAF14866.1.
AK022656 mRNA. Translation: BAB14160.1.
CR457141 mRNA. Translation: CAG33422.1.
BC001317 mRNA. Translation: AAH01317.1.
BC065815 mRNA. Translation: AAH65815.1.
AF177286 mRNA. Translation: AAQ13671.1. Sequence problems.
CCDSiCCDS3594.1. [Q9UHY7-1]
RefSeqiNP_001278946.1. NM_001292017.1.
NP_067027.1. NM_021204.4. [Q9UHY7-1]
UniGeneiHs.18442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YNSX-ray1.70A1-261[»]
1ZS9X-ray1.70A1-261[»]
ProteinModelPortaliQ9UHY7.
SMRiQ9UHY7. Positions 4-257.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121811. 26 interactions.
IntActiQ9UHY7. 10 interactions.
MINTiMINT-1415620.
STRINGi9606.ENSP00000273920.

PTM databases

DEPODiQ9UHY7.

Polymorphism and mutation databases

BioMutaiENOPH1.
DMDMi74735024.

Proteomic databases

EPDiQ9UHY7.
MaxQBiQ9UHY7.
PaxDbiQ9UHY7.
PRIDEiQ9UHY7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000273920; ENSP00000273920; ENSG00000145293. [Q9UHY7-1]
ENST00000505846; ENSP00000427209; ENSG00000145293. [Q9UHY7-2]
GeneIDi58478.
KEGGihsa:58478.
UCSCiuc003hmv.4. human. [Q9UHY7-1]

Organism-specific databases

CTDi58478.
GeneCardsiENOPH1.
HGNCiHGNC:24599. ENOPH1.
HPAiCAB004985.
HPA044607.
HPA050480.
neXtProtiNX_Q9UHY7.
PharmGKBiPA162385052.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2630. Eukaryota.
COG4229. LUCA.
GeneTreeiENSGT00440000039914.
HOGENOMiHOG000237286.
HOVERGENiHBG054539.
InParanoidiQ9UHY7.
KOiK09880.
OMAiPYAKQNV.
OrthoDBiEOG7BP83J.
PhylomeDBiQ9UHY7.
TreeFamiTF105939.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00876.
UPA00904; UER00877.
BRENDAi3.1.3.77. 2681.
ReactomeiR-HSA-1237112. Methionine salvage pathway.

Miscellaneous databases

ChiTaRSiENOPH1. human.
EvolutionaryTraceiQ9UHY7.
GenomeRNAii58478.
NextBioi64922.
PROiQ9UHY7.

Gene expression databases

BgeeiQ9UHY7.
CleanExiHS_ENOPH1.
ExpressionAtlasiQ9UHY7. baseline and differential.
GenevisibleiQ9UHY7. HS.

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]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01691. enolase-ppase. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hypothalamus.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Uterus.
  5. Qin B.M., Sheng H., Liu B., Zhao B., Liu Y.Q., Wang X.Y., Zhang Q., Song L., Liu B.H., Lu H., Xu H.S., Zheng W.Y., Gong J., Hui R.T.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 72-261 (ISOFORM 1).
    Tissue: Aorta.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Crystal structure of human E1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase activity."
    Wang H., Pang H., Bartlam M., Rao Z.
    J. Mol. Biol. 348:917-926(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND SUBSTRATE ANALOG, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiENOPH_HUMAN
AccessioniPrimary (citable) accession number: Q9UHY7
Secondary accession number(s): Q7Z4C5, Q9BVC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.