(data stored in ACNUC8465 zone)

SWISSPROT: MTNB_CANGA

ID   MTNB_CANGA              Reviewed;         208 AA.
AC   Q6FJA5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 79.
DE   RecName: Full=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   Name=MDE1 {ECO:0000255|HAMAP-Rule:MF_03116};
GN   OrderedLocusNames=CAGL0M07876g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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). {ECO:0000255|HAMAP-Rule:MF_03116}.
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-D-ribulose 1-phosphate = 5-
CC       (methylthio)-2,3-dioxopentyl phosphate + H(2)O.
CC       {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-
CC       Rule:MF_03116};
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. {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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03116}.
DR   EMBL; CR380959; CAG62665.1; -; Genomic_DNA.
DR   RefSeq; XP_449689.1; XM_449689.1.
DR   ProteinModelPortal; Q6FJA5; -.
DR   SMR; Q6FJA5; -.
DR   STRING; 284593.XP_449689.1; -.
DR   EnsemblFungi; CAG62665; CAG62665; CAGL0M07876g.
DR   KEGG; cgr:CAGL0M07876g; -.
DR   CGD; CAL0136527; MDE1.
DR   EuPathDB; FungiDB:CAGL0M07876g; -.
DR   eggNOG; KOG2631; Eukaryota.
DR   eggNOG; COG0235; LUCA.
DR   HOGENOM; HOG000192424; -.
DR   InParanoid; Q6FJA5; -.
DR   KO; K08964; -.
DR   OMA; GHGLYTW; -.
DR   OrthoDB; EOG092C44XE; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000002428; Chromosome M.
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:UniProtKB-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; SSF53639; 1.
DR   TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJA5.
DR   SWISS-2DPAGE; Q6FJA5.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; Lyase;
KW   Metal-binding; Methionine biosynthesis; Reference proteome; Zinc.
FT   CHAIN         1    208       Methylthioribulose-1-phosphate
FT                                dehydratase.
FT                                /FTId=PRO_0000393816.
FT   ACT_SITE    120    120       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   METAL        97     97       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   METAL        99     99       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   METAL       171    171       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   BINDING      79     79       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03116}.
SQ   SEQUENCE   208 AA;  23526 MW;  55C04B013F6F5998 CRC64;
     MGEAAELICT LCKQFYHLNW CTGTGGGISI RERNGESDVA YIAPSGVQKE LMRPEDLFVM
     DLIKGDYLSI PRGLKPSACT PLFLACYKKR NSGAVIHTHS QNAVMCSLLF DKEFKISNIE
     QIKAMPNHGY YDTLTIPIIE NMAHEDELID QLNDVLDKYS QDTVAVIVRR HGIFVWGPSI
     EKCKIYNEAI DYLLELALKM HQYNIPLP
//

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