Q9UHY7 (ENOPH_HUMAN) 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
MASA homolog

Gene names

Name:	ENOPH1
Synonyms:	MASA
ORF Names:	MSTP145

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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). Ref.7
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.
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. Ref.7
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family.
Sequence caution	The sequence AAQ13671.1 differs from that shown. Reason: Frameshift at position 235.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-methionine salvage from methylthioadenosine Inferred from direct assay Ref.7. Source: UniProtKB polyamine metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acireductone synthase activity Inferred from direct assay Ref.7. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglycolate phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UHY7-1)

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: Q9UHY7-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 261

261

Enolase-phosphatase E1 HAMAP-Rule MF_03117

PRO_0000254007

Regions

Region

153 – 154

2

Substrate binding HAMAP-Rule MF_03117

Sites

Metal binding

16

1

Magnesium

Metal binding

18

1

Magnesium; via carbonyl oxygen

Metal binding

212

1

Magnesium

Binding site

187

1

Substrate

Natural variations

Alternative sequence

1 – 146

146

Missing in isoform 2.

VSP_021160

Secondary structure

1

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261

Helix Strand Turn

Details...

Beta strand

12 – 15

4

Turn

19 – 21

3

Helix

24 – 29

6

Helix

31 – 46

16

Helix

50 – 65

16

Turn

66 – 68

3

Helix

83 – 103

21

Helix

108 – 123

16

Helix

135 – 144

10

Beta strand

148 – 152

5

Helix

157 – 165

9

Helix

173 – 175

3

Beta strand

177 – 180

4

Helix

182 – 184

3

Helix

190 – 200

11

Helix

204 – 206

3

Beta strand

207 – 212

6

Helix

214 – 222

9

Beta strand

226 – 230

5

Helix

240 – 245

6

Beta strand

248 – 251

4

Helix

252 – 254

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 12B3F73463907E2C	FASTA	261	28,933
	10 20 30 40 50 60 MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR 70 80 90 100 110 120 KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA 130 140 150 160 170 180 AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF 190 200 210 220 230 240 DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD 250 260 DEKTYYSLIT SFSELYLPSS T
	Isoform 2 [UniParc]. Checksum: 43E2FD7570657AFC	FASTA	115	12,552
	10 20 30 40 50 60 MKVYIYSSGS VEAQKLLFGH STEGDILELV DGHFDTKIGH KVESESYRKI ADSIGCSTNN 70 80 90 100 110 ILFLTDVTRE ASAAEEADVH VAVVVRPGNA GLTDDEKTYY SLITSFSELY LPSST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00038378.
IPI00795241.

RefSeq

NP_067027.1. NM_021204.3.

UniGene

Hs.18442.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YNS	X-ray	1.70	A	1-261	[»]
1ZS9	X-ray	1.70	A	1-261	[»]

ProteinModelPortal

Q9UHY7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UHY7. 1 interaction.

MINT

MINT-1415620.

STRING

9606.ENSP00000273920.

Polymorphism databases

DMDM

74735024.

Proteomic databases

PaxDb

Q9UHY7.

PRIDE

Q9UHY7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000273920; ENSP00000273920; ENSG00000145293.
ENST00000505846; ENSP00000427209; ENSG00000145293.

GeneID

58478.

KEGG

hsa:58478.

UCSC

uc003hmv.3. human.
uc003hmx.3. human.

Organism-specific databases

CTD

58478.

GeneCards

GC04P083351.

HGNC

HGNC:24599. ENOPH1.

HPA

CAB004985.
HPA044607.

neXtProt

NX_Q9UHY7.

PharmGKB

PA162385052.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4229.

HOGENOM

HOG000237286.

HOVERGEN

HBG054539.

InParanoid

Q9UHY7.

KO

K09880.

OMA

EDRKSTA.

OrthoDB

EOG405S1X.

PhylomeDB

Q9UHY7.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

UniPathway

UPA00904; UER00876.
UPA00904; UER00877.

Gene expression databases

ArrayExpress

Q9UHY7.

Bgee

Q9UHY7.

CleanEx

HS_ENOPH1.

Genevestigator

Q9UHY7.

GermOnline

ENSG00000145293. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1000. 1 hit.

HAMAP

MF_03117. Salvage_MtnC_euk.

InterPro

IPR023943. Enolase-ppase_E1.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA_v1.
[Graphical view]

Pfam

PF13419. HAD_2. 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...

Other

EvolutionaryTrace

Q9UHY7.

GenomeRNAi

58478.

NextBio

64922.

Entry information

Entry name

ENOPH_HUMAN

Accession

Primary (citable) accession number: Q9UHY7
Secondary accession number(s): Q7Z4C5, Q9BVC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.