ID I4VK07_9GAMM Unreviewed; 186 AA.
AC I4VK07;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=UU9_15767 {ECO:0000313|EMBL:EIL87548.1};
OS Rhodanobacter fulvus Jip2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163408 {ECO:0000313|EMBL:EIL87548.1, ECO:0000313|Proteomes:UP000004210};
RN [1] {ECO:0000313|EMBL:EIL87548.1, ECO:0000313|Proteomes:UP000004210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jip2T {ECO:0000313|Proteomes:UP000004210};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL87548.1}.
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DR EMBL; AJXU01000075; EIL87548.1; -; Genomic_DNA.
DR RefSeq; WP_007082780.1; NZ_AJXU01000075.1.
DR AlphaFoldDB; I4VK07; -.
DR STRING; 1163408.UU9_15767; -.
DR PATRIC; fig|1163408.3.peg.3201; -.
DR eggNOG; COG1791; Bacteria.
DR OrthoDB; 9795636at2; -.
DR UniPathway; UPA00904; UER00878.
DR Proteomes; UP000004210; 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; ACIREDUCTONE DIOXYGENASE; 1.
DR PANTHER; PTHR23418:SF0; 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:UP000004210}.
FT BINDING 97
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT BINDING 97
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT BINDING 99
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT BINDING 99
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT BINDING 103
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT BINDING 103
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT BINDING 141
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT BINDING 141
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT SITE 96
FT /note="May play a role in metal incorporation in vivo"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT SITE 102
FT /note="May play a role in transmitting local conformational
FT changes"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
FT SITE 105
FT /note="Important to generate the dianion"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01682"
SQ SEQUENCE 186 AA; 20956 MW; 76D779495722D7B0 CRC64;
MSQLRIFDEA QPQAALAEHR DHAAIARELG KVGVRFERWE ASQPIEPGAS QDEVIAAYRG
DIDRLMAEKG YQSVDVISLT PDHPDRATLR QKFLSEHTHS EDEVRFFVAG AGQFTLHIND
KVYDVLCEKG DLIGVPDGTP HWFDMSESPY FVAIRLFTNK EGWVAQFTGT DLASRFPRMS
PLVHTS
//
