ID   ENOPH_BOVIN             Reviewed;         261 AA.
AC   Q0VD27;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   05-MAY-2009, entry version 23.
DE   RecName: Full=Enolase-phosphatase E1;
DE            EC=3.1.3.77;
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase;
DE   AltName: Full=MASA homolog;
GN   Name=ENOPH1; Synonyms=MASA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme that enolizes the substrate to form
CC       the intermediate 2-hydroxy-5-(methylthio)-3-oxopent-1-enyl
CC       phosphate, which is then dephosphorylated to form the acireductone
CC       1,2-dihydroxy-5-(methylthio)pent-1-en-3-one (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5-(methylthio)-2,3-dioxopentyl phosphate +
CC       H(2)O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from (S)-methyl-5-thio-alpha-D-
CC       ribose 1-phosphate: step 3/6.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from (S)-methyl-5-thio-alpha-D-
CC       ribose 1-phosphate: step 4/6.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       MasA/mtnC family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC119871; AAI19872.1; -; mRNA.
DR   IPI; IPI00685778; -.
DR   RefSeq; NP_001069343.1; -.
DR   UniGene; Bt.3244; -.
DR   SMR; Q0VD27; 4-257.
DR   Ensembl; ENSBTAG00000014805; Bos taurus.
DR   GeneID; 525563; -.
DR   KEGG; bta:525563; -.
DR   HOVERGEN; Q0VD27; -.
DR   OMA; Q0VD27; AHWEEEE.
DR   BRENDA; 3.1.3.77; 251.
DR   GO; GO:0043874; F:acireductone synthase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019509; P:methionine salvage; ISS:UniProtKB.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR010041; Enolase_ppase.
DR   InterPro; IPR006439; HAD-SF_hydro_IA_v1.
DR   PANTHER; PTHR20371; Enolase_ppase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Hydrolase; Magnesium; Metal-binding;
KW   Methionine biosynthesis.
FT   CHAIN         1    261       Enolase-phosphatase E1.
FT                                /FTId=PRO_0000254006.
FT   REGION      153    154       Substrate binding (By similarity).
FT   COMPBIAS     48     51       Poly-Glu.
FT   METAL        16     16       Magnesium (By similarity).
FT   METAL        18     18       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       212    212       Magnesium (By similarity).
FT   BINDING     187    187       Substrate (By similarity).
SQ   SEQUENCE   261 AA;  28930 MW;  D6288757291FAC10 CRC64;
     MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYVKENVE EYLQAHWEEE ECQQDVRLLR
     KQAEEDSHLD GAVPIPAASG NGADDPQWMI QAVVDNVYWQ MSLDRKTTAL KQLQGHMWRA
     AFKAGHMKAE FFEDVVPAVR KWREAGMKVY VYSSGSVEAQ KLLFGHSTEG DILELVDGHF
     DTKIGHKVES ESYQKIASSI GCSTNNILFL TDVSREASAA EEAGVHVAVV VRPGNAGLTD
     DEKTHFSLIT SFSELYLPSS T
//