ID A0A4U6THT1_SETVI Unreviewed; 522 AA.
AC A0A4U6THT1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 08-OCT-2025, entry version 21.
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};
GN ORFNames=SEVIR_8G127700v2 {ECO:0000313|EMBL:TKW00684.1};
OS Setaria viridis (Green bristlegrass) (Setaria italica subsp. viridis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4556 {ECO:0000313|EMBL:TKW00684.1, ECO:0000313|Proteomes:UP000298652};
RN [1] {ECO:0000313|EMBL:TKW00684.1, ECO:0000313|Proteomes:UP000298652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. A10 {ECO:0000313|Proteomes:UP000298652};
RA Huang P., Jenkins J., Grimwood J., Barry K., Healey A., Mamidi S.,
RA Sreedasyam A., Shu S., Feldman M., Wu J., Yu Y., Chen C., Johnson J.,
RA Rokhsar D., Baxter I., Schmutz J., Brutnell T., Kellogg E.;
RT "WGS assembly of Setaria viridis.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM016559; TKW00684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U6THT1; -.
DR Gramene; TKW00684; TKW00684; SEVIR_8G127700v2.
DR OMA; IPNGCHA; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000298652; Chromosome 8.
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 HAMAP; MF_01681; Salvage_MtnC; 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:UP000298652};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03118}.
FT DOMAIN 36..239
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT REGION 1..247
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT REGION 283..522
FT /note="Enolase-phosphatase E1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT ACT_SITE 162
FT /note="Proton donor/acceptor; for methylthioribulose-1-
FT phosphate dehydratase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 119
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 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 421..422
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 455
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03118"
SQ SEQUENCE 522 AA; 57151 MW; CE2379E729323532 CRC64;
MSCGGCACDA AAAGTGATAS ASEAYLQGEP VREARELVAE LCRHFYAQGW VTGTGGSITV
KVNDPAVPLA DRLIVMSPSG VQKERMVAED MYVMAADGKV LSAPSAKPWP NKPPKCTDCA
PLFLKAYLMR GAGAVIHSHG METCIATMLN PGAKEFRMTH MEMIKGIKGH GYRDELVIPI
IENTPYEYEL TDSLSEAIAA YPKATAVLVR NHGIYVWGDS WINAKTQAEC YHYLLDACIK
LYQLGIDWAT PEHGPINSAK RLRSILSPEI PNGCHAAESS KCVVLDIEGT TTPISFVTDV
MFPYARDNVR KHLTSTFDSE ETKEDIKLLR IQTEDDLRNG IAGAVPVPPD EAGKEEVINS
LVANVESMIK ADRKITPLKQ LQGHIWRTGF EKKELQGVVF EDVPVALKNW HASGIKVYIY
SSGSREAQRL LFGNTTHGDL RKFLCGYFDT TTGNKRETKS YFEISQSLGV DSPSQILFIT
DVFQEAVAAK NAGFDVIISI RPGNAPLPDN HGFRTIKSFS EI
//
