ID W9IMD6_FUSOX Unreviewed; 191 AA.
AC W9IMD6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 08-NOV-2023, entry version 22.
DE SubName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000313|EMBL:EWY93696.1};
GN ORFNames=FOYG_06780 {ECO:0000313|EMBL:EWY93696.1};
OS Fusarium oxysporum NRRL 32931.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY93696.1, ECO:0000313|Proteomes:UP000030753};
RN [1] {ECO:0000313|EMBL:EWY93696.1, ECO:0000313|Proteomes:UP000030753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH717842; EWY93696.1; -; Genomic_DNA.
DR AlphaFoldDB; W9IMD6; -.
DR OrthoDB; 275419at2759; -.
DR Proteomes; UP000030753; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:InterPro.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 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 NCBIfam; TIGR03328; salvage_mtnB; 1.
DR PANTHER; PTHR10640; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR PANTHER; PTHR10640:SF7; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000030753};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 4..170
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 191 AA; 21896 MW; B91F93B060201EFA CRC64;
MKNTDIYVMA LSEQDPNHNK LNQRTYLRSP PCYKPSQCTP LFLAAFTRRG AGCCIHTHSQ
WAVLVTLLLE SQGPGKDRVF EINNIEQIKG FGRGMNKTGN LGYHDTLRIP VIENTPHEED
LTEYLEEAMD KYPDTYAVLV RRHGVYVWGD NVHKAKTQCE SLDYLFQLAV EMKKLGLPWI
SEVEQIAPQR T
//
