(data stored in ACNUC30567 zone)

HOGENOM: AEDAE_4337_PE9

ID   AEDAE_4337_PE9                       STANDARD;      PRT;   243 AA.
AC   AEDAE_4337_PE9; Q16NX0; Q16NW8; Q16NX1; Q16NX2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable methylthioribulose-1-phosphate dehydratase;
DE   Short=MTRu-1-P dehydratase; EC=4.2.1 109; (AEDAE_4337.PE9).
GN   ORFNames=AAEL011830;
OS   AEDES AEGYPTI.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera;
OC   Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae;
OC   Culicini; Aedes.
OX   NCBI_TaxID=7159;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_4337.PE9.
CC       Aedes aegypti supercontig supercont1.619 AaegL1 full sequence 1..686650
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MTNB_AEDAE
CC   -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-
CC       phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-
CC       phosphate (DK-MTP-1-P) (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-D-ribulose 1-phosphate = 5-
CC       (methylthio)-2,3-dioxopentyl phosphate + H(2)O.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: step 2/6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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         Note=Produced by alternative initiation at Met-103 of isoform F;
CC   -!- SIMILARITY: Belongs to the aldolase class II family. MtnB
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000192424 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL011830;AAEL011830-RF;AAEL011830-PF .
DR   EMBL; CH477804; - ;
DR   UniProtKB/Swiss-Prot; Q16NX0; Q16NW8; Q16NX1; Q16NX2; -.
DR   EMBL; CH477804; EAT36055.1; -; Genomic_DNA.
DR   EMBL; CH477804; EAT36056.1; -; Genomic_DNA.
DR   EMBL; CH477804; EAT36057.1; -; Genomic_DNA.
DR   EMBL; CH477804; EAT36054.1; -; Genomic_DNA.
DR   EMBL; CH477804; EAT36052.1; -; Genomic_DNA.
DR   EMBL; CH477804; EAT36053.1; -; Genomic_DNA.
DR   RefSeq; XP_001655750.1; XM_001655700.1.
DR   RefSeq; XP_001655751.1; XM_001655701.1.
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   UniGene; Aae.6734; -.
DR   ProteinModelPortal; Q16NX0; -.
DR   STRING; Q16NX0; -.
DR   EnsemblMetazoa; AAEL011830-RF; AAEL011830-PF ; AAEL011830.
DR   GeneID; 5575432; -.
DR   KEGG; aag:AaeL_AAEL011830; -.
DR   VectorBase; AAEL011830; Aedes aegypti.
DR   OMA; THSQHAV; -.
DR   OrthoDB; EOG44MW80; -.
DR   PhylomeDB; Q16NX0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:EC.
DR   GO; GO:0071267; P:L-methionine salvage; IEA:InterPro.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR   Gene3D; G3DSA:3.40.225.10; Aldolase_II/adducin_N; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SUPFAM; SSF53639; Aldolase_II_N; 1.
DR   TIGRFAMs; TIGR03328; Salvage_mtnB; 1.
DR   HOGENOMDNA; AEDAE_4337.PE9; -.
KW   AAEL0118303; AAEL011830-PF ; Q16NX0; Q16NW7; CH477804;
KW   Alternative initiation; Alternative splicing; Amino-acid biosynthesis;
KW   Cytoplasm; Lyase; Metal-binding; Methionine biosynthesis; Zinc.
SQ   SEQUENCE   243 AA;  UNKNOWN MW;  UNKNOWN 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
//

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