MTNB_NAEGR
ID MTNB_NAEGR Reviewed; 240 AA.
AC D2VN51;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Probable methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03116};
GN ORFNames=NAEGRDRAFT_70372;
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30224 / NEG-M;
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate
CC (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_03116}.
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_03116};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03116};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03116};
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_03116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03116}.
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DR EMBL; GG738884; EFC41682.1; -; Genomic_DNA.
DR AlphaFoldDB; D2VN51; -.
DR SMR; D2VN51; -.
DR STRING; 5762.XP_002674426.1; -.
DR EnsemblProtists; EFC41682; EFC41682; NAEGRDRAFT_70372.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_70372; -.
DR eggNOG; KOG2631; Eukaryota.
DR InParanoid; D2VN51; -.
DR OMA; IRGHGLY; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR InterPro; IPR027514; Salvage_MtnB_euk.
DR PANTHER; PTHR10640; PTHR10640; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Lyase; Metal-binding;
KW Methionine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..240
FT /note="Probable methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000393859"
FT ACT_SITE 150
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ SEQUENCE 240 AA; 27164 MW; A2EBEBA42D5D22C1 CRC64;
MSQQSTAVKV FDHTQLNDTH TPQQVIVELM KLYYTQGWVS GTGGGISMKK DGKIYIAPSG
IHKERIKEDQ IFVMEQDPEV QVVDIQSCQH LKTVYSPNDN GYNFKISACQ PLFQLCYDVR
GAGAVIHSHA LSAMLATLIY DKEFKVTHLE MIKGIRGHGF YDELVVPIIE NTAFENELAG
SLKEALEKYP NTFAVLVKRH GVYIWGKDWV EAKTHAEVYH YLFDCAVRMK QLGFDASSKQ