ID MTNC_SYNP2 Reviewed; 228 AA.
AC B1XPT1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 02-NOV-2016, entry version 59.
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=SYNPCC7002_A0552;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C.,
RA Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) 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: 5-(methylthio)-2,3-dioxopentyl phosphate +
CC H(2)O = 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one + phosphate.
CC {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; CP000951; ACA98559.1; -; Genomic_DNA.
DR RefSeq; WP_012306183.1; NC_010475.1.
DR ProteinModelPortal; B1XPT1; -.
DR STRING; 32049.SYNPCC7002_A0552; -.
DR EnsemblBacteria; ACA98559; ACA98559; SYNPCC7002_A0552.
DR KEGG; syp:SYNPCC7002_A0552; -.
DR PATRIC; 23815568; VBISynSp37135_0744.
DR eggNOG; ENOG4106YVY; Bacteria.
DR eggNOG; COG4229; LUCA.
DR HOGENOM; HOG000237286; -.
DR KO; K09880; -.
DR OMA; ALQGIIW; -.
DR OrthoDB; POG091H0FHU; -.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0043715; F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0043874; F:acireductone synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01681; Salvage_MtnC; 1.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Hydrolase; Magnesium;
KW Metal-binding; Methionine biosynthesis; Reference proteome.
FT CHAIN 1 228 Enolase-phosphatase E1.
FT /FTId=PRO_0000357420.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1 224 ihamap:Salvage_MtnC [T]
SQ SEQUENCE 228 AA; 25394 MW; 3D07289441EE3ED5 CRC64;
MIQFVLMDIE GTTTSVSFVF DVLFPYFRDN IQSIASRAEE PEIAAILKQV QDLALTETGT
SLDQTGAIAT LHQWSVEDRK VAPLKAMQGF LWEEGYKNGD FRGHVYPDVL PKLKEWQKEG
IQLGIYSSGS VKAQKLLFGY SDYGDLTGYF DYFFDLKVGQ KRDVQSYQAI AQAVQLPPEA
ILFLSDVPAE LDAAIQAGYQ AWQLVRPGTT ASPTHQQVTD FGAITSLH
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