ID MTNB_DROGR Reviewed; 230 AA.
AC B4JLL3;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 29-MAY-2013, entry version 34.
DE RecName: Full=Probable methylthioribulose-1-phosphate dehydratase;
DE Short=MTRu-1-P dehydratase;
DE EC=4.2.1.109;
GN ORFNames=GH11851;
OS Drosophila grimshawi (Fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 -!- SIMILARITY: Belongs to the aldolase class II family. MtnB
CC subfamily.
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DR EMBL; CH916370; EDW00466.1; -; Genomic_DNA.
DR RefSeq; XP_001991841.1; XM_001991805.1.
DR STRING; 7222.FBpp0145757; -.
DR EnsemblMetazoa; FBtr0147265; FBpp0145757; FBgn0119330.
DR GeneID; 6564975; -.
DR KEGG; dgr:Dgri_GH11851; -.
DR FlyBase; FBgn0119330; Dgri\GH11851.
DR eggNOG; COG0235; -.
DR InParanoid; B4JLL3; -.
DR KO; K08964; -.
DR OMA; ELCRLFY; -.
DR OrthoDB; EOG44MW80; -.
DR UniPathway; UPA00904; UER00875.
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:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_03116; Salvage_MtnB_euk; 1; -.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
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; Aldolase_II_N; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Lyase;
KW Metal-binding; Methionine biosynthesis; Zinc.
FT CHAIN 1 230 Probable methylthioribulose-1-phosphate
FT dehydratase.
FT /FTId=PRO_0000393782.
FT METAL 105 105 Zinc (By similarity).
FT METAL 107 107 Zinc (By similarity).
SQ SEQUENCE 230 AA; 26319 MW; E079EDF1E12D75A3 CRC64;
MALSFFKDLP EEHPRHLIPA LCRQFYHLGW VTGTGGGMSI KQDNEIYIAP SGVQKERMQP
EDLFVQNIDG KDLQLPPEIK GLSKSQCTPL FMLAYRHRNA GAVIHTHSQH AVMATLLWPG
KTFRCTHLEM IKGIFDEADE RYLRYDEQLI VPIIENTPHE RDLADSMYAA MMEYPGCSAV
LVRRHGVYVW GKTWEKAKTM SECYDYLFSI AVQMKKAGLN PEKFEKPSLG
//
