(data stored in SCRATCH zone)

SWISSPROT: MTND_ASPFU

ID   MTND_ASPFU              Reviewed;         176 AA.
AC   Q4WDE1;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase {ECO:0000255|HAMAP-Rule:MF_03154};
DE            EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_03154};
DE   AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_03154};
GN   Name=adi1; ORFNames=AFUA_6G04430;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Catalyzes the formation of formate and 2-keto-4-
CC       methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene
CC       (DHK-MTPene). {ECO:0000255|HAMAP-Rule:MF_03154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-
CC         methylsulfanyl-2-oxobutanoate + formate + 2 H(+);
CC         Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252;
CC         EC=1.13.11.54; Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC       Note=Binds 1 Fe cation per monomer. Can also use other divalent metal
CC       cations. {ECO:0000255|HAMAP-Rule:MF_03154};
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 5/6. {ECO:0000255|HAMAP-Rule:MF_03154}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}.
CC   -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC       {ECO:0000255|HAMAP-Rule:MF_03154}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL85597.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AAHF01000012; EAL85597.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_747635.1; XM_742542.1.
DR   STRING; 746128.CADAFUBP00009123; -.
DR   GeneID; 3505296; -.
DR   KEGG; afm:AFUA_6G04430; -.
DR   EuPathDB; FungiDB:Afu6g04430; -.
DR   HOGENOM; HOG000201071; -.
DR   InParanoid; Q4WDE1; -.
DR   KO; K08967; -.
DR   OrthoDB; 1166094at2759; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000002530; Chromosome 6.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
DR   GO; GO:0006555; P:methionine metabolic process; IBA:GO_Central.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_03154; Salvage_MtnD_euk; 1.
DR   InterPro; IPR004313; ARD.
DR   InterPro; IPR027496; ARD_euk.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR23418; PTHR23418; 1.
DR   Pfam; PF03079; ARD; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDE1.
DR   SWISS-2DPAGE; Q4WDE1.
KW   Amino-acid biosynthesis; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW   Methionine biosynthesis; Nucleus; Oxidoreductase; Reference proteome.
FT   CHAIN           1..176
FT                   /note="1,2-dihydroxy-3-keto-5-methylthiopentene
FT                   dioxygenase"
FT                   /id="PRO_0000414362"
FT   METAL           81
FT                   /note="Iron or nickel"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   METAL           83
FT                   /note="Iron or nickel"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   METAL           87
FT                   /note="Iron or nickel"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   METAL           126
FT                   /note="Iron or nickel"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
SQ   SEQUENCE   176 AA;  20848 MW;  88B020A256BABBB8 CRC64;
     MKAYWYDNKP GDQREPHDSG RPVTVDYLAS IGVQYYHFPS LESVNELAKE RGYKNRDEIV
     VSPQAMGDVY EEKVKMFFNE HLHEDEEIRY IRDGEGYFDV RGQEDEWVRI KLAKDDLIIL
     PAGIYHRFTT DDKNYVKAMR LFQEEPKWTP LNRGPDVDEN SHRQSYLRTI QNKTVA
//

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