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MTND_ACICJ
ID   MTND_ACICJ              Reviewed;         180 AA.
AC   A5FUG5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Acry_0018;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes 2 different reactions between oxygen 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(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC       Note=Binds 1 Fe(2+) cation per monomer. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; CP000697; ABQ29247.1; -; Genomic_DNA.
DR   RefSeq; WP_011941212.1; NC_009484.1.
DR   AlphaFoldDB; A5FUG5; -.
DR   SMR; A5FUG5; -.
DR   STRING; 349163.Acry_0018; -.
DR   EnsemblBacteria; ABQ29247; ABQ29247; Acry_0018.
DR   KEGG; acr:Acry_0018; -.
DR   eggNOG; COG1791; Bacteria.
DR   HOGENOM; CLU_125400_0_0_5; -.
DR   OMA; TTHWFDM; -.
DR   OrthoDB; 1964262at2; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000000245; 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   CDD; cd02232; cupin_ARD; 1.
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;
KW   Amino-acid biosynthesis; Dioxygenase; Iron; Metal-binding;
KW   Methionine biosynthesis; Nickel; Oxidoreductase; Reference proteome.
FT   CHAIN           1..180
FT                   /note="Acireductone dioxygenase"
FT                   /id="PRO_0000359168"
FT   BINDING         97
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         97
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         99
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         99
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         103
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         103
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         141
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         141
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            96
FT                   /note="May play a role in metal incorporation in vivo"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            102
FT                   /note="May play a role in transmitting local conformational
FT                   changes"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            105
FT                   /note="Important to generate the dianion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
SQ   SEQUENCE   180 AA;  19872 MW;  922893E6E7DC3130 CRC64;
     MSTLRIFDDA NPDAPLVATS DAARMAAELK SIGVRFERWE SPVAIAADAS PEEILEAYRP
     YLDRLMGETG AGSADVIKMT PDHPQAGTLR EKFLNEHIHT EDEVRFFVRG SGHFVMHLDG
     KVYDAYCTEG DLISVPANTR HWFDAGSTPD FIALRIFTDT SGWVAHFTGD QISARFPVAA
 
 
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