MTNB_AEDAE
ID MTNB_AEDAE Reviewed; 243 AA.
AC Q16NX0; J9HZP4; Q16NW8; Q16NX1; Q16NX2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=AAEL011830;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=F;
CC IsoId=Q16NX0-1; Sequence=Displayed;
CC Name=D;
CC IsoId=Q16NX0-2; Sequence=VSP_039058;
CC Name=C;
CC IsoId=Q16NX0-3; Sequence=VSP_039058, VSP_039059;
CC Name=E;
CC IsoId=Q16NX0-4; Sequence=VSP_039057;
CC -!- MISCELLANEOUS: [Isoform E]: Produced by alternative initiation at Met-
CC 103 of isoform F. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03116}.
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DR EMBL; CH477804; EAT36052.1; -; Genomic_DNA.
DR EMBL; CH477804; EAT36054.1; -; Genomic_DNA.
DR EMBL; CH477804; EAT36055.1; -; Genomic_DNA.
DR EMBL; CH477804; EAT36056.1; -; Genomic_DNA.
DR EMBL; CH477804; EAT36057.1; -; Genomic_DNA.
DR EMBL; CH477804; EJY57940.1; -; Genomic_DNA.
DR RefSeq; XP_001655750.1; XM_001655700.1.
DR RefSeq; XP_001655752.1; XM_001655702.1.
DR RefSeq; XP_001655753.1; XM_001655703.1.
DR RefSeq; XP_001655754.1; XM_001655704.1.
DR RefSeq; XP_001655755.1; XM_001655705.1.
DR RefSeq; XP_011492975.1; XM_011494673.1.
DR AlphaFoldDB; Q16NX0; -.
DR SMR; Q16NX0; -.
DR STRING; 7159.AAEL011830-PF; -.
DR GeneID; 5575432; -.
DR KEGG; aag:5575432; -.
DR VEuPathDB; VectorBase:AAEL011830; -.
DR eggNOG; KOG2631; Eukaryota.
DR InParanoid; Q16NX0; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; 1062330at2759; -.
DR PhylomeDB; Q16NX0; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000008820; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
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 Alternative initiation; Alternative splicing; Amino-acid biosynthesis;
KW Cytoplasm; Lyase; Metal-binding; Methionine biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..243
FT /note="Probable methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000393778"
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_039057"
FT VAR_SEQ 1..22
FT /note="MNLQVRLQDAALDGVGNHRHRM -> MALLRSSFQDYSE (in isoform
FT C and isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_039058"
FT VAR_SEQ 93..128
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_039059"
SQ SEQUENCE 243 AA; 28074 MW; 04AD779B956CE934 CRC64;
MNLQVRLQDA ALDGVGNHRH RMEHPRKLIP ELCKQFYNLG WVTGTGGGIS IKLDDEIYIA
PSGVQKERIL PDDLFIQNID GDDLQLPPDY KKLTKSQCTP LFMLAYREKN AGAVIHTHSQ
SAVIATLVWP GREFRCTHLE MIKGIYDHEL GRYLRFDEEL IVPIIENTPF EKDLEQRMEH
AMKEYPGSSA VLVRRHGIYV WGHTWQKAKA MAECYDYLFS LTVEMKKLGL DPNDIPKYYR
SNK
