MTBC_POPTR
ID MTBC_POPTR Reviewed; 518 AA.
AC B9N1F9; U5GWH5;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 79.
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=POPTR_0001s40980g;
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nisqually;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S.,
RA Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S.,
RA Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M.,
RA Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B.,
RA Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D.,
RA Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J.,
RA Tuskan G., Rokhsar D.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; CM009290; ERP66814.1; -; Genomic_DNA.
DR RefSeq; XP_006370245.1; XM_006370183.1.
DR AlphaFoldDB; B9N1F9; -.
DR SMR; B9N1F9; -.
DR STRING; 3694.POPTR_0001s40980.1; -.
DR EnsemblPlants; PNT59237; PNT59237; POPTR_001G399000v3.
DR GeneID; 18095573; -.
DR Gramene; PNT59237; PNT59237; POPTR_001G399000v3.
DR KEGG; pop:18095573; -.
DR eggNOG; KOG2630; Eukaryota.
DR eggNOG; KOG2631; Eukaryota.
DR HOGENOM; CLU_023273_3_1_1; -.
DR InParanoid; B9N1F9; -.
DR OMA; RNNVGRH; -.
DR UniPathway; UPA00904; UER00875.
DR UniPathway; UPA00904; UER00876.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000006729; Chromosome 1.
DR ExpressionAtlas; B9N1F9; baseline.
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_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; 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; 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..518
FT /note="Probable bifunctional methylthioribulose-1-phosphate
FT dehydratase/enolase-phosphatase E1"
FT /id="PRO_0000394160"
FT REGION 1..247
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT REGION 279..518
FT /note="Enolase-phosphatase E1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT ACT_SITE 162
FT /note="Proton donor/acceptor; for methylthioribulose-1-
FT phosphate dehydratase activity"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_03118"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 417..418
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 451
FT /ligand="substrate"
FT /ligand_label="2"
FT /ligand_note="for enolase-phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03118"
SQ SEQUENCE 518 AA; 56863 MW; C6E68E5CF992444A CRC64;
MAAAPPAVAV NGGGMAAAKV ASQAYLESKA VKDTRVLIAD LCKQFYTLGW VSGTGGSITI
KAHDDSIPKR QQLILMSPSG VQKERMEPED MYVLATNGSI LSSPSPKPYP YKPPKCSDCA
PLFLKAYDMR NAGAVIHSHG MESCLVTMIN PLSKEFRITH MEMIKGIQGH GYYDELVVPI
IENTAYENEL TDSLAKAIEA YPKTTAVLVR NHGIYIWGDS WISAKTQAEC YHYLFDAAIK
LHQIGLDWST PNHGPIQNVK VKAGMNNSNN RIEPLPRCIV LDIEGTTTPI TFVADVLFPY
ARDNVGRHLS ATYDTAETKD DINLLRTQVE DDLAQGVDGA IPIPTDDAGK EEVIAALVAN
VEAMIKADRK ITALKQLQGH IWRTGYENNE LEGVVYDDVP EALEKWHALG IKVYIYSSGS
RLAQRLIFGK TNYGDLRKYL SGFFDTTVGN KKETRSYIEI SESLGVDKPS DILFVTDVFQ
EAFAAKGAGL DVMISIRPGN APLPENHGFK TITSFAEI
