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Acireductone dioxygenase (1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase) (DHK-MTPene dioxygenase) (Acireductone dioxygenase (Fe(2 )-requiring)) (ARD') (Fe-ARD) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2 )-requiring)) (ARD) (Ni-ARD) (EC 1.13.11.53)

 MTND_LEPBA              Reviewed;         177 AA.
B0SFU6;
20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
20-JAN-2009, sequence version 2.
23-MAY-2018, entry version 60.
RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
AltName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
Short=DHK-MTPene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
Short=ARD' {ECO:0000255|HAMAP-Rule:MF_01682};
Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_01682};
AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
Short=ARD {ECO:0000255|HAMAP-Rule:MF_01682};
Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_01682};
Name=mtnD {ECO:0000255|HAMAP-Rule:MF_01682};
OrderedLocusNames=LBF_1254;
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
NCBI_TaxID=355278;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Patoc 1 / Ames;
PubMed=18270594; DOI=10.1371/journal.pone.0001607;
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C.,
McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z.,
Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
"Genome sequence of the saprophyte Leptospira biflexa provides
insights into the evolution of Leptospira and the pathogenesis of
leptospirosis.";
PLoS ONE 3:E1607-E1607(2008).
-!- FUNCTION: Catalyzes 2 different reactions between oxygene and the
acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)
depending upon the metal bound in the active site. Fe-containing
acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-
methylthiobutyrate (KMTB), the alpha-ketoacid precursor of
methionine in the methionine recycle pathway. Ni-containing
acireductone dioxygenase (Ni-ARD) produces methylthiopropionate,
carbon monoxide and formate, and does not lie on the methionine
recycle pathway. {ECO:0000255|HAMAP-Rule:MF_01682}.
-!- CATALYTIC ACTIVITY: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one +
O(2) = 3-(methylthio)propanoate + formate + CO.
{ECO:0000255|HAMAP-Rule:MF_01682}.
-!- CATALYTIC ACTIVITY: 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one +
O(2) = 4-(methylthio)-2-oxobutanoate + formate.
{ECO:0000255|HAMAP-Rule:MF_01682}.
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
Note=Binds 1 Fe cation per monomer. {ECO:0000255|HAMAP-
Rule:MF_01682};
-!- COFACTOR:
Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
Note=Binds 1 nickel ion per monomer. {ECO:0000255|HAMAP-
Rule:MF_01682};
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
1-phosphate: step 5/6. {ECO:0000255|HAMAP-Rule:MF_01682}.
-!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01682}.
-!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
{ECO:0000255|HAMAP-Rule:MF_01682}.
-!- SEQUENCE CAUTION:
Sequence=ABZ93776.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; CP000777; ABZ93776.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_041769985.1; NC_010842.1.
ProteinModelPortal; B0SFU6; -.
SMR; B0SFU6; -.
PRIDE; B0SFU6; -.
EnsemblBacteria; ABZ93776; ABZ93776; LBF_1254.
GeneID; 35830091; -.
KEGG; lbf:LBF_1254; -.
HOGENOM; HOG000201072; -.
KO; K08967; -.
OrthoDB; POG091H0K83; -.
UniPathway; UPA00904; UER00878.
GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:UniProtKB-EC.
GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IEA:UniProtKB-EC.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:InterPro.
Gene3D; 2.60.120.10; -; 1.
HAMAP; MF_01682; Salvage_MtnD; 1.
InterPro; IPR004313; ARD.
InterPro; IPR023956; ARD_bac.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR011051; RmlC_Cupin_sf.
PANTHER; PTHR23418; PTHR23418; 1.
Pfam; PF03079; ARD; 1.
SUPFAM; SSF51182; SSF51182; 1.
3: Inferred from homology;
Amino-acid biosynthesis; Dioxygenase; Iron; Metal-binding;
Methionine biosynthesis; Nickel; Oxidoreductase.
CHAIN 1 177 Acireductone dioxygenase.
/FTId=PRO_0000359202.
METAL 97 97 Iron; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
METAL 97 97 Nickel; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
METAL 99 99 Iron; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
METAL 99 99 Nickel; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
METAL 103 103 Iron; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
METAL 103 103 Nickel; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
METAL 141 141 Iron; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
METAL 141 141 Nickel; alternate. {ECO:0000255|HAMAP-
Rule:MF_01682}.
SITE 105 105 Important to generate the dianion.
{ECO:0000255|HAMAP-Rule:MF_01682}.
SEQUENCE 177 AA; 20227 MW; 8535BCA7A1337D38 CRC64;
MATIVKKQET IQDKDQVKAY LTQKGLVYES YKTPESLDLI LGQKGLSDAE KEEVLSGLEY
RFDQLKKQHG YKANDLVVLH DEVPGISDML AKFDKLHIHT DEEVRYIIDG SGIFGFIIDG
ERFEVHVGKG DFISIPANTN HWFTLDQTMR IKAVRYFKDN SGWTPVYVDE SKVLINA


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