Q8BGB7 (ENOPH_MOUSE) 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
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

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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-methionine salvage from methylthioadenosine Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acireductone synthase activity Inferred from sequence or structural similarity. 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: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 257	257	Enolase-phosphatase E1 HAMAP-Rule MF_03117		PRO_0000254008
Regions
	Region	150 – 151	2	Substrate binding By similarity
Sites
	Metal binding	16	1	Magnesium By similarity
	Metal binding	18	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	209	1	Magnesium By similarity
	Binding site	184	1	Substrate By similarity
Natural variations
	Alternative sequence	55 – 85	31	Missing in isoform 2.		VSP_021161
Experimental info
	Sequence conflict	56	1	V → I in AAH21429. Ref.2
	Sequence conflict	74	1	P → L in AAH21429. Ref.2
	Sequence conflict	152	1	G → R in BAB26606. Ref.1
	Sequence conflict	236	1	T → N in BAE35014. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: AD64B1C70976C344	FASTA	257	28,600
	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
	Isoform 2 [UniParc]. Checksum: C8DBC7513DB08943	FASTA	226	25,359
	10 20 30 40 50 60 MVVVSVPAEV TVILLDIEGT TTPIAFVKDV LFPYIKENVK EYLQTHWEEE ECQQMIQAVV 70 80 90 100 110 120 DNVYWQMSHD RKTTALKQLQ GHMWKAAFTA GRMKAEFFAD VVPAVRRWRE AGMKVYIYSS 130 140 150 160 170 180 GSVEAQKLLF GHSTEGDILE LIDGHFDTKI GHKVDSESYR KIADSIGCST NNILFLTDVT 190 200 210 220 VEASAAEEAD VHVAVVVRPG NAGLTDDEKT YYNLITSFSE LYLPST

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. , 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.
IPI	IPI00653664. IPI00798544.
RefSeq	NP_001156507.1. NM_001163035.1. NP_080697.2. NM_026421.3.
UniGene	Mm.11311.
3D structure databases
HSSP	HSSP built from PDB template 1YNS based on UniProtKB Q9UHY7.
ProteinModelPortal	Q8BGB7.
SMR	Q8BGB7. Positions 4-254.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000031268.
Proteomic databases
PaxDb	Q8BGB7.
PRIDE	Q8BGB7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031268; ENSMUSP00000031268; ENSMUSG00000029326. ENSMUST00000169390; ENSMUSP00000129704; ENSMUSG00000029326.
GeneID	67870.
KEGG	mmu:67870.
UCSC	uc008yha.2. mouse. uc012dzq.1. mouse.
Organism-specific databases
CTD	58478.
MGI	MGI:1915120. Enoph1.
Phylogenomic databases
eggNOG	COG4229.
GeneTree	ENSGT00440000039914.
HOGENOM	HOG000237286.
HOVERGEN	HBG054539.
InParanoid	Q8BGB7.
KO	K09880.
OMA	THWEEDE.
OrthoDB	EOG405S1X.
Enzyme and pathway databases
UniPathway	UPA00904; UER00876. UPA00904; UER00877.
Gene expression databases
Bgee	Q8BGB7.
CleanEx	MM_ENOPH1.
Genevestigator	Q8BGB7.
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
ChiTaRS	ENOPH1. mouse.
NextBio	325783.
SOURCE	Search...

Entry information

Entry name

ENOPH_MOUSE

Accession

Primary (citable) accession number: Q8BGB7
Secondary accession number(s): Q3TGK8 , Q3TXA2, Q3U8Y4, Q8VC92, Q9D6U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program