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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
