Reviewed, UniProtKB/Swiss-Prot Q8BGB7 (ENOPH_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Bifunctional enzyme that enolizes the substrate to form the intermediate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one By similarity.
Catalytic activity	5-(methylthio)-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.
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. 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.
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
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Gene Ontology (GO)
Biological process	methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine salvage Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	acireductone synthase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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		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. 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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. NP_080697.2.
UniGene	Mm.11311
3D structure databases
SMR	Q8BGB7. Positions 4-254.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BGB7.
Proteomic databases
PRIDE	Q8BGB7.
Genome annotation databases
Ensembl	ENSMUST00000031268; ENSMUSP00000031268; ENSMUSG00000029326; Mus musculus. [Genome view]
GeneID	67870.
NMPDR	fig|10090.3.peg.11952.
UCSC	uc008yha.1. mouse.
Organism-specific databases
CTD	67870.
MGI	MGI:1915120. Enoph1.
Phylogenomic databases
HOVERGEN	Q8BGB7.
OMA	AHWEEEE.
Enzyme and pathway databases
BRENDA	3.1.3.77. 244.
Gene expression databases
ArrayExpress	Q8BGB7.
Bgee	Q8BGB7.
CleanEx	MM_ENOPH1.
Genevestigator	Q8BGB7.
Family and domain databases
InterPro	IPR005834. Dehalogen-like_hydro. IPR010041. Enolase_ppase. IPR006439. HAD-SF_hydro_IA_v1. [Graphical view]
PANTHER	PTHR20371. Enolase_ppase. 1 hit.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01691. enolase-ppase. 1 hit. TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNet	Search...
Other Resources
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:	November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)