(data stored in ACNUC29543 zone)

SWISSPROT: MTNC_SYNR3

ID   MTNC_SYNR3              Reviewed;         249 AA.
AC   A5GR42;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_01681};
DE            EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_01681};
DE   AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_01681};
GN   Name=mtnC {ECO:0000255|HAMAP-Rule:MF_01681};
GN   OrderedLocusNames=SynRCC307_0448;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the enolization of
CC       2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the
CC       intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
CC       (HK-MTPenyl-1-P), which is then dephosphorylated to form the
CC       acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-
CC       MTPene). {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-
CC         dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC         Xref=Rhea:RHEA:21700, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:49252, ChEBI:CHEBI:58828; EC=3.1.3.77;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01681};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01681};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01681};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: step 3/6. {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: step 4/6. {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01681}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       MasA/MtnC family. {ECO:0000255|HAMAP-Rule:MF_01681}.
DR   EMBL; CT978603; CAK27351.1; -; Genomic_DNA.
DR   SMR; A5GR42; -.
DR   STRING; 316278.SynRCC307_0448; -.
DR   EnsemblBacteria; CAK27351; CAK27351; SynRCC307_0448.
DR   KEGG; syr:SynRCC307_0448; -.
DR   eggNOG; ENOG4106YVY; Bacteria.
DR   eggNOG; COG4229; LUCA.
DR   HOGENOM; HOG000237286; -.
DR   KO; K09880; -.
DR   OMA; HMWRAAY; -.
DR   UniPathway; UPA00904; UER00876.
DR   UniPathway; UPA00904; UER00877.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   CDD; cd01629; HAD_EP; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_01681; Salvage_MtnC; 1.
DR   InterPro; IPR023943; Enolase-ppase_E1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   Pfam; PF13419; HAD_2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01691; enolase-ppase; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GR42.
DR   SWISS-2DPAGE; A5GR42.
KW   Amino-acid biosynthesis; Complete proteome; Hydrolase; Magnesium;
KW   Metal-binding; Methionine biosynthesis; Reference proteome.
FT   CHAIN         1    249       Enolase-phosphatase E1.
FT                                /FTId=PRO_0000357423.
SQ   SEQUENCE   249 AA;  27233 MW;  DBA4F9D2FEE0CD60 CRC64;
     MIDWESLRAI VLDIEGTTCP VDFVTGSLFP YARQHLGTLL SQDDQQAPLK PLLDEVRIAW
     KHENSAEAPA YSDSQDPLAL LPYLQWLIDQ DRKLAPLKEL QGLTWRHGYQ SGALTTPLFA
     DVAPALKRWQ QRGLRLAVYS SGSVAAQQLF YGHTSDGDLS DLFERWYDTR LGPKNEAQSY
     TLLAADLQLP AHAVLFISDS SGELAAAQAA GLQICGSQRP GNPETLSAKW PVVVSSLEAL
     APSGPPGLR
//

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