(data stored in SCRATCH3701 zone)

SWISSPROT: MTND_SYNS3

ID   MTND_SYNS3              Reviewed;         202 AA.
AC   Q0ICL5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE   AltName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=DHK-MTPene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE   AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=ARD' {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE            EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_01682};
DE   AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE            EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_01682};
GN   Name=mtnD {ECO:0000255|HAMAP-Rule:MF_01682}; OrderedLocusNames=sync_0589;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Catalyzes 2 different reactions between oxygene and the
CC       acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)
CC       depending upon the metal bound in the active site. Fe-containing
CC       acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-
CC       methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine
CC       in the methionine recycle pathway. Ni-containing acireductone
CC       dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and
CC       formate, and does not lie on the methionine recycle pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_01682}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-
CC         (methylsulfanyl)propanoate + CO + formate + 2 H(+);
CC         Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016,
CC         ChEBI:CHEBI:49252; EC=1.13.11.53; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01682};
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_01682};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC       Note=Binds 1 Fe cation per monomer. {ECO:0000255|HAMAP-Rule:MF_01682};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC       Note=Binds 1 nickel ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01682};
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_01682}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01682}.
CC   -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01682}.
DR   EMBL; CP000435; ABI47203.1; -; Genomic_DNA.
DR   RefSeq; WP_011618534.1; NC_008319.1.
DR   SMR; Q0ICL5; -.
DR   STRING; 64471.sync_0589; -.
DR   EnsemblBacteria; ABI47203; ABI47203; sync_0589.
DR   KEGG; syg:sync_0589; -.
DR   eggNOG; ENOG4108CAF; Bacteria.
DR   eggNOG; COG1791; LUCA.
DR   HOGENOM; HOG000201072; -.
DR   KO; K08967; -.
DR   OMA; TTHWFDM; -.
DR   OrthoDB; 1964262at2; -.
DR   BioCyc; SSP64471:G1G72-570-MONOMER; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000001961; Chromosome.
DR   GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_01682; Salvage_MtnD; 1.
DR   InterPro; IPR004313; ARD.
DR   InterPro; IPR023956; ARD_bac.
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; Q0ICL5.
DR   SWISS-2DPAGE; Q0ICL5.
KW   Amino-acid biosynthesis; Dioxygenase; Iron; Metal-binding;
KW   Methionine biosynthesis; Nickel; Oxidoreductase; Reference proteome.
FT   CHAIN           1..202
FT                   /note="Acireductone dioxygenase"
FT                   /id="PRO_0000359239"
FT   METAL           110
FT                   /note="Iron; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   METAL           110
FT                   /note="Nickel; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   METAL           112
FT                   /note="Iron; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   METAL           112
FT                   /note="Nickel; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   METAL           116
FT                   /note="Iron; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   METAL           116
FT                   /note="Nickel; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   METAL           154
FT                   /note="Iron; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   METAL           154
FT                   /note="Nickel; alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            109
FT                   /note="May play a role in metal incorporation in vivo"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            115
FT                   /note="May play a role in transmitting local conformational
FT                   changes"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            118
FT                   /note="Important to generate the dianion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
SQ   SEQUENCE   202 AA;  22643 MW;  7605FD2908F3F7AB CRC64;
     MTELRIYATR GAGVEADRDS AVAAAPEALL STSNAEQISA QLKTRGIKFQ RWPSKPKLEQ
     GAMQEQILEA YASLIASVQK NEGYQTVDVM RVERDQISGS TLRQTFRQEH QHAEDEVRFF
     VEGCGLFALH IKDEVLQVIC EANDWIAIPA GTRHWFDMGV DPNYCVIRFF KNSGGWAASF
     THDPIADHYP GLDQARKQTT QG
//

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