MTBC_RICCO
ID MTBC_RICCO Reviewed; 527 AA.
AC B9SQI7;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 {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 ORFNames=RCOM_0591060;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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}.
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DR EMBL; EQ974085; EEF34141.1; -; Genomic_DNA.
DR RefSeq; XP_002528256.1; XM_002528210.2.
DR AlphaFoldDB; B9SQI7; -.
DR SMR; B9SQI7; -.
DR STRING; 3988.XP_002528256.1; -.
DR PRIDE; B9SQI7; -.
DR GeneID; 8265316; -.
DR KEGG; rcu:8265316; -.
DR eggNOG; KOG2630; Eukaryota.
DR eggNOG; KOG2631; Eukaryota.
DR InParanoid; B9SQI7; -.
DR OrthoDB; 436252at2759; -.
DR UniPathway; UPA00904; UER00875.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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 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 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..527
FT /note="Probable bifunctional methylthioribulose-1-phosphate
FT dehydratase/enolase-phosphatase E1"
FT /id="PRO_0000394161"
FT REGION 1..244
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT REGION 288..527
FT /note="Enolase-phosphatase E1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT ACT_SITE 159
FT /note="Proton donor/acceptor; for methylthioribulose-1-
FT phosphate dehydratase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 116
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 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 426..427
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 460
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
SQ SEQUENCE 527 AA; 57738 MW; E33FAF2B5F97F669 CRC64;
MAAAAAPAVA VNGGVKVASQ AYLESKAVKE TRVLISDLCR QFYNLGWVSG TGGSITIKVH
DDSIPKPNQL ILMSPSGVQK ERMEPEDMYV LAANGSILSS PSPKPYPHKP PKCSDCGPLF
LKAYEMCNAG AVIHSHGMES CLVTMINPLS KEFKITHMEM IKGIKGHGYY DELVVPIIEN
TAYENELTDS LAKAIEEYPK TTAVLVRNHG IYIWGDSWIS AKTQAECYHY LFDAAIKLHQ
LGLDWSTPNH GLIQNVKALI GSNRDINTSV KAGLKDSNHG MQSLPGCIVL DIEGTTTPIT
FVADVLFPYA RDNVGRHLYA TYETAETQDD IKLLRTQVED DLARGVNEAV SIPPDDAGKE
EVIAALVANV EAMIKADRKI TALKQLQGHI WRTGFQNNEL EGVVYDDVPE ALEKWHALGI
KVYIYSSGSR LAQRLIFGKT NYGDLRKYLS GFFDTTVGNK RETRSYIEIS ESVGVDRPSE
ILFVTDVVQE AVAAKGAGLE AVISIRQGNA PLPENHGFKT INSLSEI
