ID A0A0D9XS40_9ORYZ Unreviewed; 511 AA.
AC A0A0D9XS40;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 18-JUN-2025, entry version 48.
DE RecName: Full=Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 {ECO:0000256|HAMAP-Rule:MF_03118};
DE Includes:
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_03118};
DE Short=MTRu-1-P dehydratase {ECO:0000256|HAMAP-Rule:MF_03118};
DE EC=4.2.1.109 {ECO:0000256|HAMAP-Rule:MF_03118};
DE Includes:
DE RecName: Full=Enolase-phosphatase E1 {ECO:0000256|HAMAP-Rule:MF_03118};
DE EC=3.1.3.77 {ECO:0000256|HAMAP-Rule:MF_03118};
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000256|HAMAP-Rule:MF_03118};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR11G10860.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR11G10860.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR11G10860.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR11G10860.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(methylsulfanyl)-D-ribulose 1-phosphate = 5-methylsulfanyl-
CC 2,3-dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58548, ChEBI:CHEBI:58828;
CC EC=4.2.1.109; Evidence={ECO:0000256|HAMAP-Rule:MF_03118};
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:0000256|HAMAP-Rule:MF_03118};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03118};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03118};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03118};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03118};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 2/6. {ECO:0000256|HAMAP-Rule:MF_03118}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 3/6. {ECO:0000256|HAMAP-Rule:MF_03118}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 4/6. {ECO:0000256|HAMAP-Rule:MF_03118}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HAD-like
CC hydrolase superfamily. MasA/MtnC family. {ECO:0000256|HAMAP-
CC Rule:MF_03118}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldolase class II
CC family. MtnB subfamily. {ECO:0000256|HAMAP-Rule:MF_03118}.
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DR AlphaFoldDB; A0A0D9XS40; -.
DR STRING; 77586.A0A0D9XS40; -.
DR EnsemblPlants; LPERR11G10860.1; LPERR11G10860.1; LPERR11G10860.
DR Gramene; LPERR11G10860.1; LPERR11G10860.1; LPERR11G10860.
DR eggNOG; KOG2630; Eukaryota.
DR eggNOG; KOG2631; Eukaryota.
DR HOGENOM; CLU_023273_3_1_1; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000032180; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
DR CDD; cd01629; HAD_EP; 1.
DR FunFam; 1.10.720.60:FF:000001; Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1; 1.
DR FunFam; 3.40.225.10:FF:000010; Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1; 1.
DR FunFam; 3.40.50.1000:FF:000088; Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1; 1.
DR Gene3D; 1.10.720.60; -; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR HAMAP; MF_03118; Salvage_MtnBC; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR InterPro; IPR027505; MtnB_viridiplantae.
DR InterPro; IPR027514; Salvage_MtnB_euk.
DR NCBIfam; TIGR01691; enolase-ppase; 1.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR03328; salvage_mtnB; 1.
DR PANTHER; PTHR20371; ENOLASE-PHOSPHATASE E1; 1.
DR PANTHER; PTHR20371:SF1; ENOLASE-PHOSPHATASE E1; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDF00044; enolase-phosphatase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03118};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03118};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03118};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03118};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03118};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03118};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_03118}; Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03118}.
FT DOMAIN 24..227
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT REGION 1..235
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT REGION 272..511
FT /note="Enolase-phosphatase E1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT ACT_SITE 150
FT /note="Proton donor/acceptor; for methylthioribulose-1-
FT phosphate dehydratase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 107
FT /ligand="substrate"
FT /ligand_label="1"
FT /ligand_note="for methylthioribulose-1-phosphate
FT dehydratase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 410..411
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 444
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
SQ SEQUENCE 511 AA; 56185 MW; 893EF1EBB76C16DC CRC64;
MACCGGATAS AAYVEGEAVR EARELVAELC RHFYLQGWVT GTGGSITVKA NDPAIPLADQ
LIVMSPSGVQ KERMVAEDMY VMSADGKLLS SPVSKPWPNK PPKCTDCAPL FMKAYLMRGA
GAVIHSHGME TCIATMLDPG AKEFRMTHME MIKGIKGHGY RDELVIPIIE NTPYEYELTE
SLAEAIAAYP KATAVLVRNH GIYVWGDSWI NAKTQAECYH YLFDAAIKLY QLGIDWTTPE
HGLLSSAKRP RSVLSSGIPN GCSDVKPSKQ CVVLDIEGTT TPISFVTDVM FPYARNNVRK
HLISTYNSDE TKEDIKLLRI QVEEDLKNGV VGSVPIPPDD AGKEEVINAI VANVESMIKA
DRKITSLKQL QGHIWRTGFE SKELQGVVFE DVPQALKHWH ASGTKVYIYS SGSREAQRLL
FGNTTYGDLR QYLCGFFDTT TGNKRETKSY SEISQALGVD SPAQILFITD VFQEAVAAKS
AGFDIIISIR PGNAPLPEDH GFRTIKSFSE I
//
