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Database: UniProt
Entry: A0A0N0N272_9ACTN
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ID   A0A0N0N272_9ACTN        Unreviewed;       199 AA.
AC   A0A0N0N272;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Acireductone dioxygenase {ECO:0000256|HAMAP-Rule:MF_01682};
DE   AltName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase {ECO:0000256|HAMAP-Rule:MF_01682};
DE            Short=DHK-MTPene dioxygenase {ECO:0000256|HAMAP-Rule:MF_01682};
DE   AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_01682};
DE            Short=ARD' {ECO:0000256|HAMAP-Rule:MF_01682};
DE            Short=Fe-ARD {ECO:0000256|HAMAP-Rule:MF_01682};
DE            EC=1.13.11.54 {ECO:0000256|HAMAP-Rule:MF_01682};
DE   AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000256|HAMAP-Rule:MF_01682};
DE            Short=ARD {ECO:0000256|HAMAP-Rule:MF_01682};
DE            Short=Ni-ARD {ECO:0000256|HAMAP-Rule:MF_01682};
DE            EC=1.13.11.53 {ECO:0000256|HAMAP-Rule:MF_01682};
GN   Name=mtnD {ECO:0000256|HAMAP-Rule:MF_01682};
GN   ORFNames=OK074_1891 {ECO:0000313|EMBL:KPI16279.1};
OS   Actinobacteria bacterium OK074.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI16279.1, ECO:0000313|Proteomes:UP000037991};
RN   [1] {ECO:0000313|EMBL:KPI16279.1, ECO:0000313|Proteomes:UP000037991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK074 {ECO:0000313|EMBL:KPI16279.1,
RC   ECO:0000313|Proteomes:UP000037991};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|ARBA:ARBA00000428,
CC         ECO:0000256|HAMAP-Rule:MF_01682};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01682};
CC       Note=Binds 1 Fe(2+) cation per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_01682};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01682};
CC       Note=Binds 1 nickel ion per monomer. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01682}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01682}.
CC   -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC       {ECO:0000256|HAMAP-Rule:MF_01682}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI16279.1}.
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DR   EMBL; LJCV01000099; KPI16279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0N272; -.
DR   PATRIC; fig|1592327.3.peg.2871; -.
DR   OrthoDB; 9795636at2; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000037991; Unassembled WGS sequence.
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; Jelly Rolls; 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:SF0; 1,2-DIHYDROXY-3-KETO-5-METHYLTHIOPENTENE DIOXYGENASE; 1.
DR   PANTHER; PTHR23418; ACIREDUCTONE DIOXYGENASE; 1.
DR   Pfam; PF03079; ARD; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01682};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW   Rule:MF_01682};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01682};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01682};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   Rule:MF_01682};
KW   Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01682};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01682}; Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT   BINDING         102
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   BINDING         102
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   BINDING         104
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   BINDING         104
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   BINDING         109
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   BINDING         109
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   BINDING         147
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   BINDING         147
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   SITE            101
FT                   /note="May play a role in metal incorporation in vivo"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   SITE            107
FT                   /note="May play a role in transmitting local conformational
FT                   changes"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT   SITE            111
FT                   /note="Important to generate the dianion"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
SQ   SEQUENCE   199 AA;  22075 MW;  1C3B74E0282CAEE0 CRC64;
     MTLLTTWAES GPETLVRRTS DPAEIAAALK PIGVRYEQWP IREDVPFDAD SETVFAAYGP
     EIEKLNAEEG FTTVDVLGLH PSDDPEYPVR AKAARAKFLQ EHTHDDDDEV RFFVSGSGIF
     YLHVNGEVHA VYCEKGDLLG VPRGTTHWFD MGTKPSFTAI RFFHEEDGWI GNFTGSTIAG
     RFPDYDTIDA GFAADRATA
//
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