MTBC1_VITVI
ID MTBC1_VITVI Reviewed; 517 AA.
AC E0CSI1; F6H233;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 1 {ECO:0000255|HAMAP-Rule:MF_03118};
DE Includes:
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03118};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03118};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03118};
DE Includes:
DE RecName: Full=Enolase-phosphatase E1 {ECO:0000255|HAMAP-Rule:MF_03118};
DE EC=3.1.3.77 {ECO:0000255|HAMAP-Rule:MF_03118};
DE AltName: Full=2,3-diketo-5-methylthio-1-phosphopentane phosphatase {ECO:0000255|HAMAP-Rule:MF_03118};
GN OrderedLocusNames=VIT_19s0014g02480;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-
CC dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_03118};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03118};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03118};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03118}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldolase class II
CC family. MtnB subfamily. {ECO:0000255|HAMAP-Rule:MF_03118}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HAD-like
CC hydrolase superfamily. MasA/MtnC family. {ECO:0000255|HAMAP-
CC Rule:MF_03118}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN595229; CCB46329.1; -; Genomic_DNA.
DR EMBL; FN597046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E0CSI1; -.
DR SMR; E0CSI1; -.
DR STRING; 29760.VIT_19s0014g02480.t01; -.
DR PRIDE; E0CSI1; -.
DR EnsemblPlants; Vitvi19g00208_t001; Vitvi19g00208_P001; Vitvi19g00208.
DR Gramene; Vitvi19g00208_t001; Vitvi19g00208_P001; Vitvi19g00208.
DR eggNOG; KOG2630; Eukaryota.
DR eggNOG; KOG2631; Eukaryota.
DR HOGENOM; CLU_023273_3_1_1; -.
DR InParanoid; E0CSI1; -.
DR UniPathway; UPA00904; UER00875.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000009183; Chromosome 19.
DR ExpressionAtlas; E0CSI1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR CDD; cd01629; HAD_EP; 1.
DR Gene3D; 3.40.225.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR HAMAP; MF_03118; Salvage_MtnBC; 1.
DR HAMAP; MF_01681; Salvage_MtnC; 1.
DR HAMAP; MF_03117; Salvage_MtnC_euk; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR023943; Enolase-ppase_E1.
DR InterPro; IPR027511; ENOPH1_eukaryotes.
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 PANTHER; PTHR10640; PTHR10640; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SFLD; SFLDF00044; enolase-phosphatase; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01691; enolase-ppase; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Lyase; Magnesium; Metal-binding;
KW Methionine biosynthesis; Multifunctional enzyme; Reference proteome; Zinc.
FT CHAIN 1..517
FT /note="Probable bifunctional methylthioribulose-1-phosphate
FT dehydratase/enolase-phosphatase E1 1"
FT /id="PRO_0000403960"
FT REGION 1..240
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT REGION 278..517
FT /note="Enolase-phosphatase E1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT ACT_SITE 155
FT /note="Proton donor/acceptor; for methylthioribulose-1-
FT phosphate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 112
FT /ligand="substrate"
FT /ligand_label="1"
FT /ligand_note="for methylthioribulose-1-phosphate
FT dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 416..417
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 450
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
SQ SEQUENCE 517 AA; 57093 MW; B5B09431206D56C3 CRC64;
MAAAALNGLK MAATSQAYLE SMPVNDTRKL LSDLCRHFYG LGWVSGTGGS ITIKVHDESI
PKPQQLIVMS PSGVQKERMV PEDMYVLSPS GCFLSSPSPK PYPNKPPKCS DCAPLFMKAY
LMRNAGAVIH SHGMESCIVT MIDPLSKEFR ITHMEMIKGI QGHGYYDELV VPIIENTAHE
RELTDALAEA IEAYPKTTAV LVRNHGIYIW GDSWIHAKTQ AECYHYLFDA AIKLYQLGLD
WSTPDHGPIK KYGGKTNMSV KAGTVNSNHE TEPSRRCIVL DIEGTTTPIS FVTDVLFPFA
RNNVSRHLAA TYETDETQDD IKLLRTQVQS DLEQGIVGAV PIPPDDAGKE EVIAALVANV
EAMIKADRKI TALKQLQGHI WRTGFQNNEL EGVVFEDVPE ALQKWHASGI KVYIYSSGSR
LAQRLLFGYT NYGDLRKYLC GFFDTTVGNK RETKSYVEIT ESVGVDKPSE ILFVTDVYQE
AVAAKAAGLE VIISIRPGNG PLPDNHGFKT ITSFSDI
